{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A0A0P0ZBS7","uniProtkbId":"MENC_GEOSE","entryAudit":{"firstPublicDate":"2022-02-23","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":35,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"o-succinylbenzoate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"OSB synthase"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"OSBS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"4.2.1.113"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"4-(2'-carboxyphenyl)-4-oxybutyric acid synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"N-acylamino acid racemase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"NAAAR"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25875730"}],"value":"N-succinylamino acid racemase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25875730"}],"value":"NSAAR"},{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"NSAR"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"5.1.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"o-succinylbenzoic acid synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"menC"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"BAT31602.1"}],"value":"NSAR"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5L1G9"},{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-D/L-phenylalanine (PubMed:25875730). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D-methionine, N-formyl-D/L-methionine, N-formyl-D/L-norleucine, N-formyl-D/L-aminobutyric acid, N-formyl-D/L-norvaline, N-formyl-D/L-homophenylalanine, N-carbamoyl-D-methionine and N-carbamoyl-D-norleucine (PubMed:25875730). May be a bifunctional enzyme involved in menaquinone biosynthesis and in an irreversible pathway for the conversion of D- to L-amino acids, thereby facilitating the survival and/or growth of the organism (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10196"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:18325"},{"database":"ChEBI","id":"CHEBI:58689"}],"ecNumber":"4.2.1.113","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-D-methionine = N-acetyl-L-methionine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:59960"},{"database":"ChEBI","id":"CHEBI:71670"},{"database":"ChEBI","id":"CHEBI:85220"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"Shows highest activity in vitro with Co(2+) and Ni(2+)."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":12.6,"unit":"mM","substrate":"N-formyl-D-methionine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":9.0,"unit":"mM","substrate":"N-formyl-L-methionine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":11.1,"unit":"mM","substrate":"N-formyl-D-norleucine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":12.5,"unit":"mM","substrate":"N-formyl-L-norleucine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":19.6,"unit":"mM","substrate":"N-formyl-D-aminobutyric acid","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":17.9,"unit":"mM","substrate":"N-formyl-L-aminobutyric acid","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":9.2,"unit":"mM","substrate":"N-formyl-D-norvaline","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":24.5,"unit":"mM","substrate":"N-formyl-L-norvaline","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":3.0,"unit":"mM","substrate":"N-formyl-D-homophenylalanine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]},{"constant":5.7,"unit":"mM","substrate":"N-formyl-L-homophenylalanine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"kcat is 74.6 sec(-1) with N-formyl-D-methionine as substrate. kcat is 52.9 sec(-1) with N-formyl-L-methionine as substrate. kcat is 12.3 sec(-1) with N-formyl-D-norleucine as substrate. kcat is 8.0 sec(-1) with N-formyl-L-norleucine as substrate. kcat is 15.2 sec(-1) with N-formyl-D-aminobutyric acid as substrate. kcat is 11.6 sec(-1) with N-formyl-L-aminobutyric acid as substrate. kcat is 11.2 sec(-1) with N-formyl-D-norvaline as substrate. kcat is 19.6 sec(-1) with N-formyl-L-norvaline as substrate. kcat is 88.4 sec(-1) with N-formyl-D-homophenylalanine as substrate. kcat is 85.5 sec(-1) with N-formyl-L-homophenylalanine as substrate."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"Optimum pH is 8.0-8.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"Optimum temperature is 55-65 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"Quinol/quinone metabolism; menaquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"value":"Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"o-succinylbenzoate synthase","featureId":"PRO_0000455099"},{"type":"Active site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}]},{"type":"Active site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}]},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01933"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Mutagenesis","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Almost loss of activity with N-formyl-D/L-methionine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"Almost loss of activity with N-formyl-D/L-methionine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"Almost loss of activity with N-formyl-D/L-methionine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Almost loss of activity with N-formyl-D/L-methionine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Almost loss of activity with N-formyl-D/L-methionine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25875730"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0474","category":"Biological process","name":"Menaquinone biosynthesis"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ETOJDUNI01FDD","citationType":"submission","authors":["Sumida Y.","Iwai S.","Nishiya Y.","Kumagai S.","Yamada H.","Azuma M."],"title":"Identification and characterization of D-succinylase, and a proposed enzymatic method for D-amino acid synthesis.","publicationDate":"OCT-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"25875730","citationType":"journal article","authors":["Soriano-Maldonado P.","Andujar-Sanchez M.","Clemente-Jimenez J.M.","Rodriguez-Vico F.","Las Heras-Vazquez F.J.","Martinez-Rodriguez S."],"citationCrossReferences":[{"database":"PubMed","id":"25875730"},{"database":"DOI","id":"10.1007/s12033-015-9839-4"}],"title":"Biochemical and mutational characterization of N-succinyl-amino acid racemase from Geobacillus stearothermophilus CECT49.","publicationDate":"2015","journal":"Mol. Biotechnol.","firstPage":"454","lastPage":"465","volume":"57"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","MUTAGENESIS OF LYS-166; ASP-191; GLU-216; ASP-241 AND LYS-265"],"referenceComments":[{"value":"CECT49","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LC090555","properties":[{"key":"ProteinId","value":"BAT31602.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A0P0ZBS7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A0P0ZBS7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00079","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA01057","properties":[{"key":"RectionId","value":"UER00165"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043748","properties":[{"key":"GoTerm","value":"F:O-succinylbenzoate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009234","properties":[{"key":"GoTerm","value":"P:menaquinone biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03317","properties":[{"key":"EntryName","value":"NAAAR"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.120","properties":[{"key":"EntryName","value":"Enolase-like C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.390.10","properties":[{"key":"EntryName","value":"Enolase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01933","properties":[{"key":"EntryName","value":"MenC_2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036849","properties":[{"key":"EntryName","value":"Enolase-like_C_sf"}]},{"database":"InterPro","id":"IPR029017","properties":[{"key":"EntryName","value":"Enolase-like_N"}]},{"database":"InterPro","id":"IPR013342","properties":[{"key":"EntryName","value":"Mandelate_racemase_C"}]},{"database":"InterPro","id":"IPR013341","properties":[{"key":"EntryName","value":"Mandelate_racemase_N"}]},{"database":"InterPro","id":"IPR047585","properties":[{"key":"EntryName","value":"MenC"}]},{"database":"InterPro","id":"IPR010197","properties":[{"key":"EntryName","value":"OSBS/NAAAR"}]},{"database":"NCBIfam","id":"TIGR01928","properties":[{"key":"EntryName","value":"menC_lowGC_arch"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48073:SF5","properties":[{"key":"EntryName","value":"O-SUCCINYLBENZOATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48073","properties":[{"key":"EntryName","value":"O-SUCCINYLBENZOATE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13378","properties":[{"key":"EntryName","value":"MR_MLE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02746","properties":[{"key":"EntryName","value":"MR_MLE_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00001","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG00180","properties":[{"key":"EntryName","value":"muconate_cycloisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00009","properties":[{"key":"EntryName","value":"o-succinylbenzoate_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00922","properties":[{"key":"EntryName","value":"MR_MLE"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51604","properties":[{"key":"EntryName","value":"Enolase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54826","properties":[{"key":"EntryName","value":"Enolase N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAINIEYVILRHLQMELKAPFTTSFGTFQRKELILVEVVDRDGVSGWGESVAFSAPWYSEETVKTNWHMLEDFLVPLALAEPIHHPEELSKRFSAIRQNNMAKAALEGAVWDLYAKRLGVPLSQALGGAKKDIEVGVSIGIQPTVADLLQVIERYVAQGYRRIKVKIKPSWDVDVIREVRRVFPDVPLMADANSAYTLVDADRLKALDEFGLLMIEQPLAADDLVDHARLQPLLQTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLGEAKRIHDLCAERGAPVWCGGMLEAGVGRAHNIAITTLENFTLPGDTAASSHYWERDIITPEVEVHGGLIRVPDAPGIGYDVDRRQVERYTQFAKVFHRTATA","length":375,"molWeight":41757,"crc64":"49894E9581844BD4","md5":"8C197B1E12FF5C55963F31F83206D1F4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":3,"Mutagenesis":5},"uniParcId":"UPI0001880070"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00344","uniProtkbId":"LDH_GEOSE","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1988-01-01","entryVersion":168,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3026926"}],"value":"L-lactate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3026926"}],"value":"L-LDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3580377"}],"value":"1.1.1.27"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3026926"}],"value":"ldh"},"synonyms":[{"value":"lct"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3580377"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"}],"value":"Catalyzes the conversion of lactate to pyruvate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-lactate + NAD(+) = pyruvate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23444"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16651"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.27","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3580377"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3580377"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1731077"}],"value":"Allosterically activated by fructose 1,6-bisphosphate (FBP). The improvement in affinity for substrate occurs in two steps; the binding of fructose 1,6-bisphosphate (FBP) to the dimer, and the dimer to tetramer conversion"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3580377"},{"evidenceCode":"ECO:0000305","source":"Reference","id":"Ref.5"}],"value":"Exists as a dimer and a tetramer (dimer of dimers). The conversion occurs via the binding of fructose 1,6-bisphosphate (FBP) to the dimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the LDH/MDH superfamily. LDH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"L-lactate dehydrogenase","featureId":"PRO_0000168328"},{"type":"Active site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"}]},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2LDB"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2LDB"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2LDB"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2LDB"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32966"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2LDB"}],"ligand":{"name":"beta-D-fructose 1,6-bisphosphate","id":"ChEBI:CHEBI:32966","note":"allosteric activator"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32966"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2330370"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2LDB"}],"ligand":{"name":"beta-D-fructose 1,6-bisphosphate","id":"ChEBI:CHEBI:32966","note":"allosteric activator"}},{"type":"Binding site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1LDN"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}]},{"type":"Mutagenesis","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"This mutant undergoes a reversible subunit assembly from dimer to tetramer. However, the tetramer mutant is much more stable than the wild type, and is destabilized rather than stabilized by binding the allosteric regulator, fructose 1,6-bisphosphate (FBP). The mutation weakens the binding of fructose 1,6-bisphosphate (FBP) to both the dimeric and tetrameric forms, and almost abolishes any stimulatory effect.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3580377"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["Q"]}},{"type":"Sequence conflict","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"in Ref. 2; AAA22567","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["H"]}},{"type":"Turn","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Turn","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Turn","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Turn","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDB"}]},{"type":"Beta strand","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Turn","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Turn","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2LDB"}]},{"type":"Beta strand","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Beta strand","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]},{"type":"Helix","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LDN"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"}],"references":[{"referenceNumber":1,"citation":{"id":"3026926","citationType":"journal article","authors":["Barstow D.A.","Clarke A.R.","Chia W.N.","Wigley D.","Sharman A.F.","Holbrook J.J.","Atkinson T.","Minton N.P."],"citationCrossReferences":[{"database":"PubMed","id":"3026926"},{"database":"DOI","id":"10.1016/0378-1119(86)90165-4"}],"title":"Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene.","publicationDate":"1986","journal":"Gene","firstPage":"47","lastPage":"55","volume":"46"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"3675869","citationType":"journal article","authors":["Zuelli F.","Weber H.","Zuber H."],"citationCrossReferences":[{"database":"PubMed","id":"3675869"},{"database":"DOI","id":"10.1515/bchm3.1987.368.2.1167"}],"title":"Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax.","publicationDate":"1987","journal":"Biol. Chem. Hoppe-Seyler","firstPage":"1167","lastPage":"1177","volume":"368"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":3,"citation":{"id":"6618448","citationType":"journal article","authors":["Tratschin J.D.","Wirz B.","Frank G.","Zuber H."],"citationCrossReferences":[{"database":"PubMed","id":"6618448"},{"database":"DOI","id":"10.1515/bchm2.1983.364.2.879"}],"title":"Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. (II) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Cyanogen bromide fragments and partial sequence.","publicationDate":"1983","journal":"Hoppe-Seyler's Z. Physiol. Chem.","firstPage":"879","lastPage":"892","volume":"364"},"referencePositions":["PARTIAL PROTEIN SEQUENCE"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"6352452","citationType":"journal article","authors":["Wirz B.","Suter F.","Zuber H."],"citationCrossReferences":[{"database":"PubMed","id":"6352452"},{"database":"DOI","id":"10.1515/bchm2.1983.364.2.893"}],"title":"Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. (III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. The complete amino-acid sequence.","publicationDate":"1983","journal":"Hoppe-Seyler's Z. Physiol. Chem.","firstPage":"893","lastPage":"909","volume":"364"},"referencePositions":["PARTIAL PROTEIN SEQUENCE"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"CI-3QMNBRG8598PD","citationType":"journal article","authors":["Clarke A.R.","Atkinson T.","Campbell J.W.","Holbrook J.J."],"title":"The assembly mechanism of the lactate dehydrogenase tetramer from Bacillus stearothermophilus; the equilibrium relationships between quaternary structure and the binding of fructose 1,6-biphosphate, NADH and oxamate.","publicationDate":"1985","journal":"Biochim. Biophys. Acta","firstPage":"387","lastPage":"396","volume":"829"},"referencePositions":["FUNCTION","ACTIVITY REGULATION","SUBUNIT"]},{"referenceNumber":6,"citation":{"id":"3580377","citationType":"journal article","authors":["Clarke A.R.","Wigley D.B.","Barstow D.A.","Chia W.N.","Atkinson T.","Holbrook J.J."],"citationCrossReferences":[{"database":"PubMed","id":"3580377"},{"database":"DOI","id":"10.1016/0167-4838(87)90234-2"}],"title":"A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure.","publicationDate":"1987","journal":"Biochim. Biophys. Acta","firstPage":"72","lastPage":"80","volume":"913"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","MUTAGENESIS OF ARG-157","SUBUNIT"]},{"referenceNumber":7,"citation":{"id":"2330370","citationType":"journal article","authors":["Piontek K.","Chakrabarti P.","Schar H.P.","Rossmann M.G.","Zuber H."],"citationCrossReferences":[{"database":"PubMed","id":"2330370"},{"database":"DOI","id":"10.1002/prot.340070108"}],"title":"Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.","publicationDate":"1990","journal":"Proteins","firstPage":"74","lastPage":"92","volume":"7"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD AND FRUCTOSE 1,6-BISPHOSPHATE","SUBUNIT"]},{"referenceNumber":8,"citation":{"id":"1731077","citationType":"journal article","authors":["Wigley D.B.","Gamblin S.J.","Turkenburg J.P.","Dodson E.J.","Piontek K.","Muirhead H.","Holbrook J.J."],"citationCrossReferences":[{"database":"PubMed","id":"1731077"},{"database":"DOI","id":"10.1016/0022-2836(92)90733-z"}],"title":"Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5-A resolution.","publicationDate":"1992","journal":"J. Mol. Biol.","firstPage":"317","lastPage":"335","volume":"223"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD; FRUCTOSE 1,6-BISPHOSPHATE AND SUBSTRATE ANALOG","ACTIVITY REGULATION","ACTIVE SITE","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M14788","properties":[{"key":"ProteinId","value":"AAA22568.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M19396","properties":[{"key":"ProteinId","value":"AAA22567.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A26053","properties":[{"key":"EntryName","value":"DEBSLF"}]},{"database":"RefSeq","id":"WP_033016716.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000001.1"}]},{"database":"PDB","id":"1LDB","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A/B/C/D=1-317"}]},{"database":"PDB","id":"1LDN","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H=1-316"}]},{"database":"PDB","id":"2LDB","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A/B/C/D=1-317"}]},{"database":"AlphaFoldDB","id":"P00344","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P00344","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"89612274","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802969at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.1.1.27","properties":[{"key":"OrganismId","value":"623"}]},{"database":"SABIO-RK","id":"P00344","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00554","properties":[{"key":"RectionId","value":"UER00611"}]},{"database":"EvolutionaryTrace","id":"P00344","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004459","properties":[{"key":"GoTerm","value":"F:L-lactate dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3580377"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"1731077"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"2330370"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006089","properties":[{"key":"GoTerm","value":"P:lactate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd05291","properties":[{"key":"EntryName","value":"HicDH_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.110.10:FF:000005","properties":[{"key":"EntryName","value":"L-lactate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000018","properties":[{"key":"EntryName","value":"Malate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.110.10","properties":[{"key":"EntryName","value":"Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00488","properties":[{"key":"EntryName","value":"Lactate_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001557","properties":[{"key":"EntryName","value":"L-lactate/malate_DH"}]},{"database":"InterPro","id":"IPR011304","properties":[{"key":"EntryName","value":"L-lactate_DH"}]},{"database":"InterPro","id":"IPR018177","properties":[{"key":"EntryName","value":"L-lactate_DH_AS"}]},{"database":"InterPro","id":"IPR022383","properties":[{"key":"EntryName","value":"Lactate/malate_DH_C"}]},{"database":"InterPro","id":"IPR001236","properties":[{"key":"EntryName","value":"Lactate/malate_DH_N"}]},{"database":"InterPro","id":"IPR015955","properties":[{"key":"EntryName","value":"Lactate_DH/Glyco_Ohase_4_C"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01771","properties":[{"key":"EntryName","value":"L-LDH-NAD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF000824","properties":[{"key":"EntryName","value":"PRK00066.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004863","properties":[{"key":"EntryName","value":"PRK06223.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43128","properties":[{"key":"EntryName","value":"L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43128:SF16","properties":[{"key":"EntryName","value":"L-LACTATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02866","properties":[{"key":"EntryName","value":"Ldh_1_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00056","properties":[{"key":"EntryName","value":"Ldh_1_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000102","properties":[{"key":"EntryName","value":"Lac_mal_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00086","properties":[{"key":"EntryName","value":"LLDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF56327","properties":[{"key":"EntryName","value":"LDH C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00064","properties":[{"key":"EntryName","value":"L_LDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDANESKAIGDAMDFNHGKVFAPKPVDIWHGDYDDCRDADLVVICAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSGTILDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKLVESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFTR","length":317,"molWeight":34863,"crc64":"4B146CF681C91046","md5":"23D5823442513D85003BED650B57D31B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":15,"Modified residue":1,"Mutagenesis":1,"Sequence conflict":1,"Turn":6,"Beta strand":14,"Helix":14},"uniParcId":"UPI00001123D8"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00512","uniProtkbId":"PFKA_GEOSE","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1989-07-01","entryVersion":175,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"pfkA"},"synonyms":[{"value":"pfk"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8136379"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8136379"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2136935"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23859543"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8136379"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.07,"unit":"mM","substrate":"ATP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8136379"}]},{"constant":0.033,"unit":"mM","substrate":"fructose 6-phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8136379"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12390023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2136935"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23859543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"2136935"}],"value":"In the R state the 6-P group of fructose 6-phosphate (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from an adjacent chain. In the T state a conformation change moves Arg-162 away from the substrate. Glu-161 takes its place, hence repelling the phosphate of ATP"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"ATP-dependent 6-phosphofructokinase","featureId":"PRO_0000111935"},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12390023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12390023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12390023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12390023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12390023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6115424"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Sequence conflict","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Sequence conflict","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{}},{"type":"Sequence conflict","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["V"]}},{"type":"Sequence conflict","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["E"]}},{"type":"Sequence conflict","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Sequence conflict","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["L"]}},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Turn","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Beta strand","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]},{"type":"Helix","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4I7E"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"2956156","citationType":"journal article","authors":["French B.A.","Chang S.H."],"citationCrossReferences":[{"database":"PubMed","id":"2956156"},{"database":"DOI","id":"10.1016/0378-1119(87)90348-9"}],"title":"Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene.","publicationDate":"1987","journal":"Gene","firstPage":"65","lastPage":"71","volume":"54"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"6447595","citationType":"journal article","authors":["Kolb E.","Hudson P.J.","Harris J.I."],"citationCrossReferences":[{"database":"PubMed","id":"6447595"},{"database":"DOI","id":"10.1111/j.1432-1033.1980.tb04754.x"}],"title":"Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus.","publicationDate":"1980","journal":"Eur. J. Biochem.","firstPage":"587","lastPage":"597","volume":"108"},"referencePositions":["PROTEIN SEQUENCE"]},{"referenceNumber":3,"citation":{"id":"8436141","citationType":"journal article","authors":["Sakai H.","Ohta T."],"citationCrossReferences":[{"database":"PubMed","id":"8436141"},{"database":"DOI","id":"10.1111/j.1432-1033.1993.tb17618.x"}],"title":"Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon.","publicationDate":"1993","journal":"Eur. J. Biochem.","firstPage":"851","lastPage":"859","volume":"211"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319"]},{"referenceNumber":4,"citation":{"id":"8136379","citationType":"journal article","authors":["Byrnes M.","Zhu X.","Younathan E.S.","Chang S.H."],"citationCrossReferences":[{"database":"PubMed","id":"8136379"},{"database":"DOI","id":"10.1021/bi00177a036"}],"title":"Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme.","publicationDate":"1994","journal":"Biochemistry","firstPage":"3424","lastPage":"3431","volume":"33"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES"]},{"referenceNumber":5,"citation":{"id":"156307","citationType":"journal article","authors":["Evans P.R.","Hudson P.J."],"citationCrossReferences":[{"database":"PubMed","id":"156307"},{"database":"DOI","id":"10.1038/279500a0"}],"title":"Structure and control of phosphofructokinase from Bacillus stearothermophilus.","publicationDate":"1979","journal":"Nature","firstPage":"500","lastPage":"504","volume":"279"},"referencePositions":["X-RAY CRYSTALLOGRAPHY"]},{"referenceNumber":6,"citation":{"id":"6115424","citationType":"journal article","authors":["Evans P.R.","Farrants G.W.","Hudson P.J."],"citationCrossReferences":[{"database":"PubMed","id":"6115424"},{"database":"DOI","id":"10.1098/rstb.1981.0059"}],"title":"Phosphofructokinase: structure and control.","publicationDate":"1981","journal":"Philos. Trans. R. Soc. Lond., B, Biol. Sci.","firstPage":"53","lastPage":"62","volume":"293"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH MAGNESIUM; ADP AND FRUCTOSE-6-PHOSPHATE"]},{"referenceNumber":7,"citation":{"id":"2136935","citationType":"journal article","authors":["Schirmer T.","Evans P.R."],"citationCrossReferences":[{"database":"PubMed","id":"2136935"},{"database":"DOI","id":"10.1038/343140a0"}],"title":"Structural basis of the allosteric behaviour of phosphofructokinase.","publicationDate":"1990","journal":"Nature","firstPage":"140","lastPage":"145","volume":"343"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ALLOSTERIC INHIBITOR"]},{"referenceNumber":8,"citation":{"id":"12390023","citationType":"journal article","authors":["Riley-Lovingshimer M.R.","Ronning D.R.","Sacchettini J.C.","Reinhart G.D."],"citationCrossReferences":[{"database":"PubMed","id":"12390023"},{"database":"DOI","id":"10.1021/bi0263412"}],"title":"Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus.","publicationDate":"2002","journal":"Biochemistry","firstPage":"12967","lastPage":"12974","volume":"41"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE"]},{"referenceNumber":9,"citation":{"id":"22212099","citationType":"journal article","authors":["Mosser R.","Reddy M.C.","Bruning J.B.","Sacchettini J.C.","Reinhart G.D."],"citationCrossReferences":[{"database":"PubMed","id":"22212099"},{"database":"DOI","id":"10.1021/bi201548p"}],"title":"Structure of the apo form of Bacillus stearothermophilus phosphofructokinase.","publicationDate":"2012","journal":"Biochemistry","firstPage":"769","lastPage":"775","volume":"51"},"referencePositions":["X-RAY CRYSTALLOGRAPHY"]},{"referenceNumber":10,"citation":{"id":"23859543","citationType":"journal article","authors":["Mosser R.","Reddy M.C.","Bruning J.B.","Sacchettini J.C.","Reinhart G.D."],"citationCrossReferences":[{"database":"PubMed","id":"23859543"},{"database":"DOI","id":"10.1021/bi4002503"}],"title":"Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase.","publicationDate":"2013","journal":"Biochemistry","firstPage":"5421","lastPage":"5429","volume":"52"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PHOSPHOENOLPYRUVIC ACID"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M15643","properties":[{"key":"ProteinId","value":"AAA22656.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D13095","properties":[{"key":"ProteinId","value":"BAA02405.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A27474","properties":[{"key":"EntryName","value":"KIBSFF"}]},{"database":"RefSeq","id":"WP_033014452.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000002.1"}]},{"database":"PDB","id":"1MTO","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.20 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H=1-319"}]},{"database":"PDB","id":"3PFK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A=1-319"}]},{"database":"PDB","id":"3U39","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.79 A"},{"key":"Chains","value":"A/B/C/D=1-319"}]},{"database":"PDB","id":"4I36","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"A/B/C/D=1-319"}]},{"database":"PDB","id":"4I4I","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.49 A"},{"key":"Chains","value":"A/B/C/D=1-319"}]},{"database":"PDB","id":"4I7E","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B/C/D=1-319"}]},{"database":"PDB","id":"4PFK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A=1-319"}]},{"database":"PDB","id":"6PFK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B/C/D=1-319"}]},{"database":"AlphaFoldDB","id":"P00512","properties":[{"key":"Description","value":"-"}]},{"database":"MDRepo","id":"P00512","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P00512","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB02726","properties":[{"key":"GenericName","value":"2-Phosphoglycolic Acid"}]},{"database":"DrugBank","id":"DB04493","properties":[{"key":"GenericName","value":"Fructose-6-phosphate"}]},{"database":"DrugBank","id":"DB09344","properties":[{"key":"GenericName","value":"Invert sugar"}]},{"database":"GeneID","id":"89612055","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802503at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.7.1.11","properties":[{"key":"OrganismId","value":"623"}]},{"database":"SABIO-RK","id":"P00512","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"EvolutionaryTrace","id":"P00512","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00763","properties":[{"key":"EntryName","value":"Bacterial_PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.450:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00339","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_B1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR012828","properties":[{"key":"EntryName","value":"PFKA_ATP_prok"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02482","properties":[{"key":"EntryName","value":"PFKA_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEALANKHTIDQRMYALSKELSI","length":319,"molWeight":34119,"crc64":"EE968D39BA30712B","md5":"56A81773EE7838E65D6EEEBAA11F523D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":16,"Sequence conflict":6,"Beta strand":11,"Helix":14,"Turn":1},"uniParcId":"UPI000011294D"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P52026","uniProtkbId":"DPO1_GEOSE","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-07-15","entryVersion":146,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"DNA polymerase I"},"shortNames":[{"value":"POL I"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9016716"}],"value":"2.7.7.7"}]}},"genes":[{"geneName":{"value":"polA"},"synonyms":[{"value":"pol"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9016716"}],"value":"In addition to polymerase activity, the recombinant enzyme has strand displacement and 5'-3' exonuclease activity, but lacks proofreading 3'-5' exonuclease activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.7","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9016716"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9016716"}],"value":"Optimum temperature is 65 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"}],"value":"Single-chain monomer with multiple functions"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"}],"value":"The enzyme from this organism does not have any 3'-5' exonuclease activity. The subtilisin large fragment (residues 289-876) has wild-type polymerase activity but no 5'-3' exonuclease activity"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the DNA polymerase type-A family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"PubMed:9016716 and PubMed:9440698 strain is not known and has been termed 'X' in this entry"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAA85558.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":876,"modifier":"EXACT"}},"description":"DNA polymerase I","featureId":"PRO_0000101234"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"5'-3' exonuclease"},{"type":"Region","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":876,"modifier":"EXACT"}},"description":"Subtilisin large fragment"},{"type":"Region","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":876,"modifier":"EXACT"}},"description":"Polymerase"},{"type":"Natural variant","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"G","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Natural variant","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"AI","alternativeSequences":["TL"]}},{"type":"Natural variant","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"S","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"V","alternativeSequences":["L"]}},{"type":"Natural variant","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"GD","alternativeSequences":["EE"]}},{"type":"Natural variant","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"H","alternativeSequences":["D"]}},{"type":"Natural variant","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"LA","alternativeSequences":["VV"]}},{"type":"Natural variant","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"R","alternativeSequences":["H"]}},{"type":"Natural variant","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"K","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"L","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"V","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"AAG","alternativeSequences":["GVD"]}},{"type":"Natural variant","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"A","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"V","alternativeSequences":["A"]}},{"type":"Natural variant","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"H","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"S","alternativeSequences":["P"]}},{"type":"Natural variant","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Natural variant","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"A","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"E","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":461,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"LM","alternativeSequences":["FL"]}},{"type":"Natural variant","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":482,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"AG","alternativeSequences":["SS"]}},{"type":"Natural variant","location":{"start":{"value":487,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"N","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":491,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Natural variant","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"A","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"Q","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"QA","alternativeSequences":["GT"]}},{"type":"Natural variant","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":516,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"R","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":536,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"TV","alternativeSequences":["VI"]}},{"type":"Natural variant","location":{"start":{"value":540,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":567,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"H","alternativeSequences":["Y"]}},{"type":"Natural variant","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Natural variant","location":{"start":{"value":596,"modifier":"EXACT"},"end":{"value":596,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"H","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":598,"modifier":"EXACT"},"end":{"value":598,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"V","alternativeSequences":["D"]}},{"type":"Natural variant","location":{"start":{"value":600,"modifier":"EXACT"},"end":{"value":600,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"G","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":605,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"M","alternativeSequences":["I"]}},{"type":"Natural variant","location":{"start":{"value":619,"modifier":"EXACT"},"end":{"value":619,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"V","alternativeSequences":["T"]}},{"type":"Natural variant","location":{"start":{"value":645,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"P","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":672,"modifier":"EXACT"},"end":{"value":672,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"I","alternativeSequences":["M"]}},{"type":"Natural variant","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":678,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"G","alternativeSequences":["D"]}},{"type":"Natural variant","location":{"start":{"value":691,"modifier":"EXACT"},"end":{"value":691,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"H","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":695,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"ED","alternativeSequences":["DE"]}},{"type":"Natural variant","location":{"start":{"value":699,"modifier":"EXACT"},"end":{"value":699,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"A","alternativeSequences":["P"]}},{"type":"Natural variant","location":{"start":{"value":728,"modifier":"EXACT"},"end":{"value":728,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":741,"modifier":"EXACT"},"end":{"value":741,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"A","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":748,"modifier":"EXACT"},"end":{"value":748,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"Q","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":751,"modifier":"EXACT"},"end":{"value":751,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":790,"modifier":"EXACT"},"end":{"value":790,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["M"]}},{"type":"Natural variant","location":{"start":{"value":812,"modifier":"EXACT"},"end":{"value":813,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"SV","alternativeSequences":["NA"]}},{"type":"Natural variant","location":{"start":{"value":816,"modifier":"EXACT"},"end":{"value":816,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"R","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"I","alternativeSequences":["M"]}},{"type":"Natural variant","location":{"start":{"value":870,"modifier":"EXACT"},"end":{"value":870,"modifier":"EXACT"}},"description":"in strain: X","featureId":"","alternativeSequence":{"originalSequence":"P","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Complete loss of 5'-3' exonuclease activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A","P"]}},{"type":"Sequence conflict","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["V"]}},{"type":"Sequence conflict","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["K"]}},{"type":"Sequence conflict","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["V"]}},{"type":"Sequence conflict","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"KW","alternativeSequences":["NG"]}},{"type":"Sequence conflict","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["AGV"]}},{"type":"Sequence conflict","location":{"start":{"value":446,"modifier":"EXACT"},"end":{"value":446,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["Q"]}},{"type":"Sequence conflict","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"in Ref. 1; AAC37139","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"QP","alternativeSequences":["HA"]}},{"type":"Sequence conflict","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":678,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["W"]}},{"type":"Sequence conflict","location":{"start":{"value":785,"modifier":"EXACT"},"end":{"value":785,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["T"]}},{"type":"Sequence conflict","location":{"start":{"value":814,"modifier":"EXACT"},"end":{"value":815,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"RL","alternativeSequences":["SV"]}},{"type":"Sequence conflict","location":{"start":{"value":828,"modifier":"EXACT"},"end":{"value":828,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["G"]}},{"type":"Sequence conflict","location":{"start":{"value":842,"modifier":"EXACT"},"end":{"value":842,"modifier":"EXACT"}},"description":"in Ref. 2; AAA85558","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["G"]}},{"type":"Sequence conflict","location":{"start":{"value":857,"modifier":"EXACT"},"end":{"value":857,"modifier":"EXACT"}},"description":"in Ref. 1; AAC37139","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1U4B"}]},{"type":"Helix","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Turn","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Turn","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":473,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":522,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":531,"modifier":"EXACT"},"end":{"value":536,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":541,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":550,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BDP"}]},{"type":"Beta strand","location":{"start":{"value":551,"modifier":"EXACT"},"end":{"value":554,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":558,"modifier":"EXACT"},"end":{"value":564,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":569,"modifier":"EXACT"},"end":{"value":582,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":583,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":590,"modifier":"EXACT"},"end":{"value":594,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Turn","location":{"start":{"value":597,"modifier":"EXACT"},"end":{"value":599,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":605,"modifier":"EXACT"},"end":{"value":609,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":612,"modifier":"EXACT"},"end":{"value":614,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":621,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":625,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1XWL"}]},{"type":"Beta strand","location":{"start":{"value":628,"modifier":"EXACT"},"end":{"value":630,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1XWL"}]},{"type":"Helix","location":{"start":{"value":631,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":635,"modifier":"EXACT"},"end":{"value":639,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":647,"modifier":"EXACT"},"end":{"value":656,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":657,"modifier":"EXACT"},"end":{"value":666,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":669,"modifier":"EXACT"},"end":{"value":676,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":681,"modifier":"EXACT"},"end":{"value":689,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":694,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":699,"modifier":"EXACT"},"end":{"value":714,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":718,"modifier":"EXACT"},"end":{"value":725,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":729,"modifier":"EXACT"},"end":{"value":742,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":744,"modifier":"EXACT"},"end":{"value":760,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":761,"modifier":"EXACT"},"end":{"value":764,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":770,"modifier":"EXACT"},"end":{"value":772,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":774,"modifier":"EXACT"},"end":{"value":777,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":781,"modifier":"EXACT"},"end":{"value":817,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":823,"modifier":"EXACT"},"end":{"value":827,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":829,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":838,"modifier":"EXACT"},"end":{"value":840,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Helix","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":853,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Beta strand","location":{"start":{"value":864,"modifier":"EXACT"},"end":{"value":871,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]},{"type":"Turn","location":{"start":{"value":872,"modifier":"EXACT"},"end":{"value":874,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1NK4"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0239","category":"Molecular function","name":"DNA-directed DNA polymerase"},{"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"7557480","citationType":"journal article","authors":["Phang S.M.","Teo C.Y.","Lo E.","Wong V.W."],"citationCrossReferences":[{"database":"PubMed","id":"7557480"},{"database":"DOI","id":"10.1016/0378-1119(95)00387-l"}],"title":"Cloning and complete sequence of the DNA polymerase-encoding gene (BstpolI) and characterisation of the Klenow-like fragment from Bacillus stearothermophilus.","publicationDate":"1995","journal":"Gene","firstPage":"65","lastPage":"68","volume":"163"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"8679703","citationType":"journal article","authors":["Riggs M.G.","Tudor S.","Sivaram M.","McDonough S.H."],"citationCrossReferences":[{"database":"PubMed","id":"8679703"},{"database":"DOI","id":"10.1016/0167-4781(96)00051-6"}],"title":"Construction of single amino acid substitution mutants of cloned Bacillus stearothermophilus DNA polymerase I which lack 5'-3' exonuclease activity.","publicationDate":"1996","journal":"Biochim. Biophys. Acta","firstPage":"178","lastPage":"186","volume":"1307"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 1-5 AND 289-293","FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS TO REMOVE 5'-3' EXONUCLEASE ACTIVITY"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"9016716","citationType":"journal article","authors":["Kiefer J.R.","Mao C.","Hansen C.J.","Basehore S.L.","Hogrefe H.H.","Braman J.C.","Beese L.S."],"citationCrossReferences":[{"database":"PubMed","id":"9016716"},{"database":"DOI","id":"10.1016/s0969-2126(97)00169-x"}],"title":"Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1-A resolution.","publicationDate":"1997","journal":"Structure","firstPage":"95","lastPage":"108","volume":"5"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"X","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"9440698","citationType":"journal article","authors":["Kiefer J.R.","Mao C.","Braman J.C.","Beese L.S."],"citationCrossReferences":[{"database":"PubMed","id":"9440698"},{"database":"DOI","id":"10.1038/34693"}],"title":"Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal.","publicationDate":"1998","journal":"Nature","firstPage":"304","lastPage":"307","volume":"391"},"referencePositions":["X-RAY CRYSTALLOGRAPHY"],"referenceComments":[{"value":"X","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U23149","properties":[{"key":"ProteinId","value":"AAA85558.1"},{"key":"Status","value":"ALT_INIT"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"L42111","properties":[{"key":"ProteinId","value":"AAC37139.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JC4286","properties":[{"key":"EntryName","value":"JC4286"}]},{"database":"PIR","id":"S70368","properties":[{"key":"EntryName","value":"S70368"}]},{"database":"PDB","id":"1L3S","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1L3T","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1L3U","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1L3V","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.71 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1L5U","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1LV5","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B=297-876"}]},{"database":"PDB","id":"1NJX","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NJY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NJZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK5","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK6","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK7","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NK9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NKB","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NKC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1NKE","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1U45","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.01 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1U47","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1U48","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1U49","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.15 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1U4B","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1UA1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1XC9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"1XWL","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"2BDP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"3BDP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"3EYZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"PDB","id":"3EZ5","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/D=299-876"}]},{"database":"PDB","id":"4BDP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=297-876"}]},{"database":"AlphaFoldDB","id":"P52026","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P52026","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB07435","properties":[{"key":"GenericName","value":"1,2,3-TRIHYDROXY-1,2,3,4-TETRAHYDROBENZO[A]PYRENE"}]},{"database":"BRENDA","id":"2.7.7.7","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"P52026","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0008408","properties":[{"key":"GoTerm","value":"F:3'-5' exonuclease activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008409","properties":[{"key":"GoTerm","value":"F:5'-3' exonuclease activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034061","properties":[{"key":"GoTerm","value":"F:DNA polymerase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8679703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9016716"}]},{"database":"GO","id":"GO:0003887","properties":[{"key":"GoTerm","value":"F:DNA-directed DNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006261","properties":[{"key":"GoTerm","value":"P:DNA-templated DNA replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006302","properties":[{"key":"GoTerm","value":"P:double-strand break repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd08637","properties":[{"key":"EntryName","value":"DNA_pol_A_pol_I_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd06140","properties":[{"key":"EntryName","value":"DNA_polA_I_Bacillus_like_exo"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd09898","properties":[{"key":"EntryName","value":"H3TH_53EXO"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd09859","properties":[{"key":"EntryName","value":"PIN_53EXO"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.20:FF:000002","properties":[{"key":"EntryName","value":"DNA polymerase I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.20:FF:000003","properties":[{"key":"EntryName","value":"DNA polymerase I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1060.10:FF:000001","properties":[{"key":"EntryName","value":"DNA polymerase I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1010:FF:000001","properties":[{"key":"EntryName","value":"DNA polymerase I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.370","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1010","properties":[{"key":"EntryName","value":"5'-nuclease"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.10","properties":[{"key":"EntryName","value":"Ribonuclease H-like superfamily/Ribonuclease H"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1060.10","properties":[{"key":"EntryName","value":"Taq DNA Polymerase, Chain T, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002562","properties":[{"key":"EntryName","value":"3'-5'_exonuclease_dom"}]},{"database":"InterPro","id":"IPR020046","properties":[{"key":"EntryName","value":"5-3_exonucl_a-hlix_arch_N"}]},{"database":"InterPro","id":"IPR002421","properties":[{"key":"EntryName","value":"5-3_exonuclease"}]},{"database":"InterPro","id":"IPR036279","properties":[{"key":"EntryName","value":"5-3_exonuclease_C_sf"}]},{"database":"InterPro","id":"IPR019760","properties":[{"key":"EntryName","value":"DNA-dir_DNA_pol_A_CS"}]},{"database":"InterPro","id":"IPR001098","properties":[{"key":"EntryName","value":"DNA-dir_DNA_pol_A_palm_dom"}]},{"database":"InterPro","id":"IPR043502","properties":[{"key":"EntryName","value":"DNA/RNA_pol_sf"}]},{"database":"InterPro","id":"IPR054690","properties":[{"key":"EntryName","value":"DNA_polI_exonuclease"}]},{"database":"InterPro","id":"IPR020045","properties":[{"key":"EntryName","value":"DNA_polI_H3TH"}]},{"database":"InterPro","id":"IPR018320","properties":[{"key":"EntryName","value":"DNA_polymerase_1"}]},{"database":"InterPro","id":"IPR002298","properties":[{"key":"EntryName","value":"DNA_polymerase_A"}]},{"database":"InterPro","id":"IPR008918","properties":[{"key":"EntryName","value":"HhH2"}]},{"database":"InterPro","id":"IPR029060","properties":[{"key":"EntryName","value":"PIN-like_dom_sf"}]},{"database":"InterPro","id":"IPR012337","properties":[{"key":"EntryName","value":"RNaseH-like_sf"}]},{"database":"InterPro","id":"IPR036397","properties":[{"key":"EntryName","value":"RNaseH_sf"}]},{"database":"NCBIfam","id":"NF004397","properties":[{"key":"EntryName","value":"polA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00593","properties":[{"key":"EntryName","value":"pola"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10133","properties":[{"key":"EntryName","value":"DNA POLYMERASE I"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10133:SF27","properties":[{"key":"EntryName","value":"DNA POLYMERASE NU"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01367","properties":[{"key":"EntryName","value":"5_3_exonuc"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02739","properties":[{"key":"EntryName","value":"5_3_exonuc_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00476","properties":[{"key":"EntryName","value":"DNA_pol_A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22619","properties":[{"key":"EntryName","value":"DNA_polI_exo1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00868","properties":[{"key":"EntryName","value":"DNAPOLI"}]},{"database":"SMART","id":"SM00474","properties":[{"key":"EntryName","value":"35EXOc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00475","properties":[{"key":"EntryName","value":"53EXOc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00279","properties":[{"key":"EntryName","value":"HhH2"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00482","properties":[{"key":"EntryName","value":"POLAc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47807","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56672","properties":[{"key":"EntryName","value":"DNA/RNA polymerases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88723","properties":[{"key":"EntryName","value":"PIN domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53098","properties":[{"key":"EntryName","value":"Ribonuclease H-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00447","properties":[{"key":"EntryName","value":"DNA_POLYMERASE_A"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKNKLVLIDGNSVAYRAFFALPLLHNDKGIHTNAVYGFTMMLNKILAEEQPTHILVAFDAGKTTFRHETFQDYKGGRQQTPPELSEQFPLLRELLKAYRIPAYELDHYEADDIIGTMAARAEREGFAVKVISGDRDLTQLASPQVTVEITKKGITDIESYTPETVVEKYGLTPEQIVDLKGLMGDKSDNIPGVPGIGEKTAVKLLKQFGTVENVLASIDEIKGEKLKENLRQYRDLALLSKQLAAICRDAPVELTLDDIVYKGEDREKVVALFQELGFQSFLDKMAVQTDEGEKPLAGMDFAIADSVTDEMLADKAALVVEVVGDNYHHAPIVGIALANERGRFFLRPETALADPKFLAWLGDETKKKTMFDSKRAAVALKWKGIELRGVVFDLLLAAYLLDPAQAAGDVAAVAKMHQYEAVRSDEAVYGKGAKRTVPDEPTLAEHLVRKAAAIWALEEPLMDELRRNEQDRLLTELEQPLAGILANMEFTGVKVDTKRLEQMGAELTEQLQAVERRIYELAGQEFNINSPKQLGTVLFDKLQLPVLKKTKTGYSTSADVLEKLAPHHEIVEHILHYRQLGKLQSTYIEGLLKVVHPVTGKVHTMFNQALTQTGRLSSVEPNLQNIPIRLEEGRKIRQAFVPSEPDWLIFAADYSQIELRVLAHIAEDDNLIEAFRRGLDIHTKTAMDIFHVSEEDVTANMRRQAKAVNFGIVYGISDYGLAQNLNITRKEAAEFIERYFASFPGVKQYMDNIVQEAKQKGYVTTLLHRRRYLPDITSRNFNVRSFAERTAMNTPIQGSAADIIKKAMIDLSVRLREERLQARLLLQVHDELILEAPKEEIERLCRLVPEVMEQAVTLRVPLKVDYHYGPTWYDAK","length":876,"molWeight":98670,"crc64":"689167A801D543E4","md5":"3D25298F567FE057DFB76A638129E150"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Region":2,"Natural variant":58,"Mutagenesis":1,"Sequence conflict":14,"Beta strand":20,"Helix":35,"Turn":4},"uniParcId":"UPI0000129760"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P83847","uniProtkbId":"MUTY_GEOSE","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":113,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25995449"}],"value":"Adenine DNA glycosylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"}],"value":"3.2.2.31"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25995449"}],"value":"oxoG:A-specific adenine glycosylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14961129"}],"value":"mutY"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14961129"}],"value":"Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product (PubMed:14961129, PubMed:25995449). 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs (PubMed:25995449). May also be able to remove adenine from A:G mispairs, although this activity may not be physiologically relevant (PubMed:14961129)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.","ecNumber":"3.2.2.31","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25995449"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"}],"value":"Binds 1 [4Fe-4S] cluster (PubMed:14961129, PubMed:25995449). The cluster has a structural role (PubMed:14961129)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the Nth/MutY family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Adenine DNA glycosylase","featureId":"PRO_0000435340"},{"type":"Domain","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"HhH","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Active site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19841264"}]},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16991"},{"database":"ChEBI","id":"CHEBI:30756"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"ligand":{"name":"DNA","id":"ChEBI:CHEBI:16991","note":"substrate"},"ligandPart":{"name":"adenine group","id":"ChEBI:CHEBI:30756","note":"mispaired A"}},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16991"},{"database":"ChEBI","id":"CHEBI:176966"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"ligand":{"name":"DNA","id":"ChEBI:CHEBI:16991","note":"substrate"},"ligandPart":{"name":"8-oxoguanine group","id":"ChEBI:CHEBI:176966"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16991"},{"database":"ChEBI","id":"CHEBI:176966"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"ligand":{"name":"DNA","id":"ChEBI:CHEBI:16991","note":"substrate"},"ligandPart":{"name":"8-oxoguanine group","id":"ChEBI:CHEBI:176966"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16991"},{"database":"ChEBI","id":"CHEBI:30756"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"ligand":{"name":"DNA","id":"ChEBI:CHEBI:16991","note":"substrate"},"ligandPart":{"name":"adenine group","id":"ChEBI:CHEBI:30756","note":"mispaired A"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16991"},{"database":"ChEBI","id":"CHEBI:30756"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"ligand":{"name":"DNA","id":"ChEBI:CHEBI:16991","note":"substrate"},"ligandPart":{"name":"adenine group","id":"ChEBI:CHEBI:30756","note":"mispaired A"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.3"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRS"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1VRL"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.3"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRS"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1VRL"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.3"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRS"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1VRL"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.3"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1RRS"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1VRL"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16991"},{"database":"ChEBI","id":"CHEBI:176966"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14961129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"ligand":{"name":"DNA","id":"ChEBI:CHEBI:16991","note":"substrate"},"ligandPart":{"name":"8-oxoguanine group","id":"ChEBI:CHEBI:176966"}},{"type":"Site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25995449"}]},{"type":"Mutagenesis","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Loss of catalytic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Loss of catalytic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Helix","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Turn","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Turn","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5KN9"}]},{"type":"Helix","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Turn","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Turn","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Beta strand","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]},{"type":"Helix","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9BS2"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"14961129","citationType":"journal article","authors":["Fromme J.C.","Banerjee A.","Huang S.J.","Verdine G.L."],"citationCrossReferences":[{"database":"PubMed","id":"14961129"},{"database":"DOI","id":"10.1038/nature02306"}],"title":"Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase.","publicationDate":"2004","journal":"Nature","firstPage":"652","lastPage":"656","volume":"427"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANT ASN-144 IN COMPLEXES WITH DUPLEX DNA CONTAINING AN A:OXOG MISPAIR AND IRON-SULFUR (4FE-4S)","FUNCTION","COFACTOR"]},{"referenceNumber":2,"citation":{"id":"19841264","citationType":"journal article","authors":["Lee S.","Verdine G.L."],"citationCrossReferences":[{"database":"PubMed","id":"19841264"},{"database":"DOI","id":"10.1073/pnas.0902908106"}],"title":"Atomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylase.","publicationDate":"2009","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"18497","lastPage":"18502","volume":"106"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND DUPLEX DNA CONTAINING THE UNCLEAVABLE NUCLEOBASE 2'-FLUORO-2'-DEOXYADENOSINE","CATALYTIC ACTIVITY","ACTIVE SITE","REACTION MECHANISM","MUTAGENESIS OF GLU-43"]},{"referenceNumber":3,"citation":{"id":"CI-1SC40OOJJBAN1","citationType":"submission","authors":["O'Shea V.L.","Cao S.","Richards J.L.","Horvath M.P.","David S.S."],"title":"Structural illumination of a mutY glycosylase reaction coordinate intermediate.","publicationDate":"JAN-2009","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND DUPLEX DNA"]},{"referenceNumber":4,"citation":{"id":"25995449","citationType":"journal article","authors":["Wang L.","Lee S.J.","Verdine G.L."],"citationCrossReferences":[{"database":"PubMed","id":"25995449"},{"database":"DOI","id":"10.1074/jbc.m115.657866"}],"title":"Structural basis for avoidance of promutagenic DNA repair by MutY adenine DNA glycosylase.","publicationDate":"2015","journal":"J. Biol. Chem.","firstPage":"17096","lastPage":"17105","volume":"290"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANT ASN-144 IN COMPLEX WITH DUPLEX DNA CONTAINING AN OXOG:C BASE PAIR AND IRON-SULFUR (4FE-4S)","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","COFACTOR","MUTAGENESIS OF ASP-144"]},{"referenceNumber":5,"citation":{"id":"CI-43P9C2IOBD0P3","citationType":"submission","authors":["Woods R.D.","O'Shea V.L.","Chu A.","Cao S.","Richards J.L.","Horvath M.P.","David S.S."],"title":"Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases.","publicationDate":"SEP-2015","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH DUPLEX DNA CONTAINING AN A:OXOG MISPAIR AND IRON-SULFUR (4FE-4S)"]}],"uniProtKBCrossReferences":[{"database":"PDB","id":"1RRQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.22 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"1RRS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"1VRL","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"3G0Q","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A=9-360"}]},{"database":"PDB","id":"4YOQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.21 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"4YPH","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.32 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"4YPR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.59 A"},{"key":"Chains","value":"A/B=1-365"}]},{"database":"PDB","id":"5KN8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.81 A"},{"key":"Chains","value":"A=1-229"}]},{"database":"PDB","id":"5KN9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.93 A"},{"key":"Chains","value":"A=1-229"}]},{"database":"PDB","id":"6Q0C","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"6U7T","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"8DVP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.54 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"8DVY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.36 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"8DW0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.68 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"8DW4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.49 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"8DW7","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.96 A"},{"key":"Chains","value":"A/D=1-365"}]},{"database":"PDB","id":"8DWD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.68 A"},{"key":"Chains","value":"A=1-365"}]},{"database":"PDB","id":"8DWE","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/D=1-365"}]},{"database":"PDB","id":"8DWF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/D=1-365"}]},{"database":"PDB","id":"9BS2","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.51 A"},{"key":"Chains","value":"A=1-363"}]},{"database":"AlphaFoldDB","id":"P83847","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"P83847","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P83847","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.2.2.31","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"P83847","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25995449"}]},{"database":"GO","id":"GO:0034039","properties":[{"key":"GoTerm","value":"F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0035485","properties":[{"key":"GoTerm","value":"F:adenine/guanine mispair binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25995449"}]},{"database":"GO","id":"GO:0019104","properties":[{"key":"GoTerm","value":"F:DNA N-glycosylase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25995449"}]},{"database":"GO","id":"GO:0032357","properties":[{"key":"GoTerm","value":"F:oxidized purine DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000701","properties":[{"key":"GoTerm","value":"F:purine-specific mismatch base pair DNA N-glycosylase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19841264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25995449"}]},{"database":"GO","id":"GO:0006284","properties":[{"key":"GoTerm","value":"P:base-excision repair"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25995449"}]},{"database":"GO","id":"GO:0006298","properties":[{"key":"GoTerm","value":"P:mismatch repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00056","properties":[{"key":"EntryName","value":"ENDO3c"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03431","properties":[{"key":"EntryName","value":"NUDIX_DNA_Glycosylase_C-MutY"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1670.10:FF:000002","properties":[{"key":"EntryName","value":"Adenine DNA glycosylase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.340.30:FF:000010","properties":[{"key":"EntryName","value":"Adenine DNA glycosylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1670.10","properties":[{"key":"EntryName","value":"Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.340.30","properties":[{"key":"EntryName","value":"Hypothetical protein, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.79.10","properties":[{"key":"EntryName","value":"Nucleoside Triphosphate Pyrophosphohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005760","properties":[{"key":"EntryName","value":"A/G_AdeGlyc_MutY"}]},{"database":"InterPro","id":"IPR011257","properties":[{"key":"EntryName","value":"DNA_glycosylase"}]},{"database":"InterPro","id":"IPR003651","properties":[{"key":"EntryName","value":"Endonuclease3_FeS-loop_motif"}]},{"database":"InterPro","id":"IPR003265","properties":[{"key":"EntryName","value":"HhH-GPD_domain"}]},{"database":"InterPro","id":"IPR023170","properties":[{"key":"EntryName","value":"HhH_base_excis_C"}]},{"database":"InterPro","id":"IPR000445","properties":[{"key":"EntryName","value":"HhH_motif"}]},{"database":"InterPro","id":"IPR044298","properties":[{"key":"EntryName","value":"MIG/MutY"}]},{"database":"InterPro","id":"IPR029119","properties":[{"key":"EntryName","value":"MutY_C"}]},{"database":"InterPro","id":"IPR015797","properties":[{"key":"EntryName","value":"NUDIX_hydrolase-like_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01084","properties":[{"key":"EntryName","value":"mutY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42944","properties":[{"key":"EntryName","value":"ADENINE DNA GLYCOSYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42944:SF1","properties":[{"key":"EntryName","value":"ADENINE DNA GLYCOSYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10576","properties":[{"key":"EntryName","value":"EndIII_4Fe-2S"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00633","properties":[{"key":"EntryName","value":"HHH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00730","properties":[{"key":"EntryName","value":"HhH-GPD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14815","properties":[{"key":"EntryName","value":"NUDIX_4"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00478","properties":[{"key":"EntryName","value":"ENDO3c"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00525","properties":[{"key":"EntryName","value":"FES"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48150","properties":[{"key":"EntryName","value":"DNA-glycosylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55811","properties":[{"key":"EntryName","value":"Nudix"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTRETERFPAREFQRDLLDWFARERRDLPWRKDRDPYKVWVSEVMLQQTRVETVIPYFEQFIDRFPTLEALADADEDEVLKAWEGLGYYSRVRNLHAAVKEVKTRYGGKVPDDPDEFSRLKGVGPYTVGAVLSLAYGVPEPAVDGNVMRVLSRLFLVTDDIAKPSTRKRFEQIVREIMAYENPGAFNEALIELGALVCTPRRPSCLLCPVQAYCQAFAEGVAEELPVKMKKTAVKQVPLAVAVLADDEGRVLIRKRDSTGLLANLWEFPSCETDGADGKEKLEQMVGEQYGLQVELTEPIVSFEHAFSHLVWQLTVFPGRLVHGGPVEEPYRLAPEDELKAYAFPVSHQRVWREYKEWASGVRRPD","length":366,"molWeight":41835,"crc64":"0D37855DFCF30C6B","md5":"700DE560F2D3CB8957DC4699029EE6FE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Active site":1,"Binding site":10,"Site":1,"Mutagenesis":2,"Helix":19,"Turn":4,"Beta strand":10},"uniParcId":"UPI0006A9CBAB"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q45515","uniProtkbId":"HYDA_GEOSE","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":115,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"D-hydantoinase"},"ecNumbers":[{"value":"3.5.2.-"}]}},"comments":[{"texts":[{"value":"Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin. Has no activity on dihydropyrimidines"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}},{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}},{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"value":"Binds 2 Zn(2+) ions per subunit. Can also use Ni(2+), Co(2+) or Mn(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"value":"Completely inhibited by p-chloromercuribenzoate and partially inhibited by metal chelating agents"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7765480"}],"value":"The optimal activity is at pH 8.8 for manganese-containing form and pH 8.5 for cobalt-containing form. The oligomer is thermostable and retains full initial activity at 40-60 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"}],"value":"Carboxylation allows a single lysine to coordinate two zinc ions"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"D-hydantoinase","featureId":"PRO_0000165933"},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K1D"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12135362"}]},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Helix","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Turn","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]},{"type":"Beta strand","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K1D"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"7765480","citationType":"journal article","authors":["Mukohara Y.","Ishikawa T.","Watabe K.","Nakamura H."],"citationCrossReferences":[{"database":"PubMed","id":"7765480"},{"database":"DOI","id":"10.1271/bbb.58.1621"}],"title":"A thermostable hydantoinase of Bacillus stearothermophilus NS1122A: cloning, sequencing, and high expression of the enzyme gene, and some properties of the expressed enzyme.","publicationDate":"1994","journal":"Biosci. Biotechnol. Biochem.","firstPage":"1621","lastPage":"1626","volume":"58"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 1-20","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"NS1122A","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"12135362","citationType":"journal article","authors":["Cheon Y.-H.","Kim H.-S.","Han K.-H.","Abendroth J.","Niefind K.","Schomburg D.","Wang J.","Kim Y."],"citationCrossReferences":[{"database":"PubMed","id":"12135362"},{"database":"DOI","id":"10.1021/bi0201567"}],"title":"Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity.","publicationDate":"2002","journal":"Biochemistry","firstPage":"9410","lastPage":"9417","volume":"41"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ZINC IONS","SUBUNIT","COFACTOR","CARBOXYLATION AT LYS-150"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"S73773","properties":[{"key":"ProteinId","value":"AAC60487.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JC2310","properties":[{"key":"EntryName","value":"JC2310"}]},{"database":"PDB","id":"1K1D","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.01 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H=1-459"}]},{"database":"AlphaFoldDB","id":"Q45515","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q45515","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB03801","properties":[{"key":"GenericName","value":"Lysine Nz-Carboxylic Acid"}]},{"database":"BRENDA","id":"3.5.2.2","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"Q45515","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016812","properties":[{"key":"GoTerm","value":"F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01314","properties":[{"key":"EntryName","value":"D-HYD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000076","properties":[{"key":"EntryName","value":"Dihydropyrimidinase like 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.40.10","properties":[{"key":"EntryName","value":"Urease, subunit C, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR011778","properties":[{"key":"EntryName","value":"Hydantoinase/dihydroPyrase"}]},{"database":"InterPro","id":"IPR011059","properties":[{"key":"EntryName","value":"Metal-dep_hydrolase_composite"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR050378","properties":[{"key":"EntryName","value":"Metallo-dep_Hydrolases_sf"}]},{"database":"NCBIfam","id":"TIGR02033","properties":[{"key":"EntryName","value":"D-hydantoinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11647:SF1","properties":[{"key":"EntryName","value":"COLLAPSIN RESPONSE MEDIATOR PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11647","properties":[{"key":"EntryName","value":"HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01979","properties":[{"key":"EntryName","value":"Amidohydro_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51338","properties":[{"key":"EntryName","value":"Composite domain of metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKLIKNGTIVTATDIYEADLLIQDGKIAVIGRNLDESGAEVIDATGCYVFPGGIDPHTHLDMPFGGTVTKDDFESGTIAAAFGGTTTIIDFCLTNKGEPLKKAIETWHNKATGKAVIDYGFHLMISEITDDVLEELPKVIEEEGITSFKVFMAYKDVFQADDGTLYRTLVAAKELGALVMVHAENGDVIDYLTKKALEDGHTDPIYHALTRPPELEGEATGRACQLTELAGSQLYVVHVSCAQAVEKIAEARNKGLNVWGETCPQYLVLDQSYLEKPNFEGAKYVWSPPLREKWHQEVLWNALKNGQLQTLGSDQCSFDFKGQKELGRGDFTKIPNGGPIIEDRVSILFSEGVKKGRITLNQFVDIVSTRIAKLFGLFPKKGTIAVGADADLVIFDPTVERVISAETHHMAVDYNPFEGMKVTGEPVSVLCRGEFVVRDKQFVGKPGYGQYVKRAKYGALMADQDVVKMS","length":471,"molWeight":51725,"crc64":"FB75A507727292FB","md5":"9F890E4FABE6B965F8C50DF7C46AE48E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":10,"Modified residue":1,"Beta strand":16,"Helix":20,"Turn":7},"uniParcId":"UPI000012CFE9"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DMM5","uniProtkbId":"MCSB_GEOSE","entryAudit":{"firstPublicDate":"2014-09-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2014-09-03","entryVersion":44,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00602"}],"value":"Protein-arginine kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"value":"2.7.14.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19498169"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30962626"}],"value":"mcsB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"value":"Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Acts exclusively on Arg residues, since it cannot phosphorylate Tyr, Ser, Thr, His, Asp and Lys. Has no free arginine kinase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-[protein] + ATP = N(omega)-phospho-L-arginyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43384"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:10533"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83226"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.14.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"value":"Appears to be allosterically activated by the binding of pArg-containing polypeptides to the pArg-binding pocket localized in the C-terminal domain of McsB"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"value":"Homodimer. Dimerization is important for full catalytic activity"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"value":"In the 3D-structure the McsB dimer adopts a flat 'domino tile' shape, with the two active sites opening on the same side. Individual subunits are composed of the N-terminal catalytic, ATP:guanido phosphotransferase domain (PD, residues 1-263) and the C-terminal dimerization domain (DD, residues 264-355), which are linearly organized in a PD-DD-DD*-PD* manner (asterisk denotes the partner protomer). The PhK-like catalytic phosphotransferase domain is structurally adapted to target protein substrates. The C-terminal DD of McsB contains a pArg-binding pocket that allows pArg-carrying proteins to allosterically enhance McsB kinase activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00602"}],"value":"Belongs to the ATP:guanido phosphotransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Protein-arginine kinase","featureId":"PRO_0000430097"},{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Phosphagen kinase C-terminal"},{"type":"Motif","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"RDXXRA motif of the pArg binding pocket involved in allosteric regulation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}]},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30962626"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00602"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30962626"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00602"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30962626"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00602"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Mutagenesis","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Loss of protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Loss of protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"Loss of protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"Loss of protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Loss of protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"Loss of protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A","D"]}},{"type":"Mutagenesis","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Abolishes dimerization. Large decrease in protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"Abolishes dimerization. Large decrease in protein kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["E"]}},{"type":"Helix","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Turn","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Turn","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Turn","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Turn","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH2"}]},{"type":"Helix","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Beta strand","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]},{"type":"Helix","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6FH1"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B4QG8IHUGH8CO","citationType":"submission","authors":["Fuhrmann J."],"publicationDate":"MAY-2014","submissionDatabase":"UniProtKB"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"19498169","citationType":"journal article","authors":["Fuhrmann J.","Schmidt A.","Spiess S.","Lehner A.","Turgay K.","Mechtler K.","Charpentier E.","Clausen T."],"citationCrossReferences":[{"database":"PubMed","id":"19498169"},{"database":"DOI","id":"10.1126/science.1170088"}],"title":"McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR.","publicationDate":"2009","journal":"Science","firstPage":"1323","lastPage":"1327","volume":"324"},"referencePositions":["FUNCTION AS AN ARGININE KINASE","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","MUTAGENESIS OF GLU-122 AND GLU-213"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"30962626","citationType":"journal article","authors":["Suskiewicz M.J.","Hajdusits B.","Beveridge R.","Heuck A.","Vu L.D.","Kurzbauer R.","Hauer K.","Thoeny V.","Rumpel K.","Mechtler K.","Meinhart A.","Clausen T."],"citationCrossReferences":[{"database":"PubMed","id":"30962626"},{"database":"DOI","id":"10.1038/s41589-019-0265-y"}],"title":"Structure of McsB, a protein kinase for regulated arginine phosphorylation.","publicationDate":"2019","journal":"Nat. Chem. Biol.","firstPage":"510","lastPage":"518","volume":"15"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF APOENZYME AND IN COMPLEXES WITH ATP ANALOG AND PHOSPHOARGININE","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","DOMAIN","SUBUNIT","MUTAGENESIS OF HIS-92; GLU-122; CYS-168; ARG-208; TYR-211; GLU-213; ARG-273 AND ARG-282"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"6FH1"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6FH2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6FH3"}]}],"uniProtKBCrossReferences":[{"database":"RefSeq","id":"WP_033017267.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000002.1"}]},{"database":"PDB","id":"6FH1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B=1-355"}]},{"database":"PDB","id":"6FH2","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.70 A"},{"key":"Chains","value":"A/B=1-355"}]},{"database":"PDB","id":"6FH3","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.85 A"},{"key":"Chains","value":"A/B=1-355"}]},{"database":"AlphaFoldDB","id":"P0DMM5","properties":[{"key":"Description","value":"-"}]},{"database":"MDRepo","id":"P0DMM5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0DMM5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9791353at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.7.14.1","properties":[{"key":"OrganismId","value":"623"}]},{"database":"GO","id":"GO:0016775","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, nitrogenous group as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:1990424","properties":[{"key":"GoTerm","value":"F:protein arginine kinase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30962626"}]},{"database":"GO","id":"GO:0046314","properties":[{"key":"GoTerm","value":"P:phosphocreatine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07930","properties":[{"key":"EntryName","value":"bacterial_phosphagen_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.590.10:FF:000007","properties":[{"key":"EntryName","value":"Protein-arginine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.590.10","properties":[{"key":"EntryName","value":"Glutamine synthetase/guanido kinase, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00602","properties":[{"key":"EntryName","value":"Prot_Arg_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023660","properties":[{"key":"EntryName","value":"Arg_Kinase"}]},{"database":"InterPro","id":"IPR000749","properties":[{"key":"EntryName","value":"ATP-guanido_PTrfase"}]},{"database":"InterPro","id":"IPR022415","properties":[{"key":"EntryName","value":"ATP-guanido_PTrfase_AS"}]},{"database":"InterPro","id":"IPR022414","properties":[{"key":"EntryName","value":"ATP-guanido_PTrfase_cat"}]},{"database":"InterPro","id":"IPR014746","properties":[{"key":"EntryName","value":"Gln_synth/guanido_kin_cat_dom"}]},{"database":"InterPro","id":"IPR060285","properties":[{"key":"EntryName","value":"McsB_C"}]},{"database":"NCBIfam","id":"NF002194","properties":[{"key":"EntryName","value":"PRK01059.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002195","properties":[{"key":"EntryName","value":"PRK01059.1-5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11547:SF38","properties":[{"key":"EntryName","value":"ARGININE KINASE 1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11547","properties":[{"key":"EntryName","value":"ARGININE OR CREATINE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00217","properties":[{"key":"EntryName","value":"ATP-gua_Ptrans"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF27454","properties":[{"key":"EntryName","value":"McsB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55931","properties":[{"key":"EntryName","value":"Glutamine synthetase/guanido kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00112","properties":[{"key":"EntryName","value":"PHOSPHAGEN_KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51510","properties":[{"key":"EntryName","value":"PHOSPHAGEN_KINASE_C"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFGKFFNTAVSAWMSQEGPNSDIVLSSRIRLARNIVDFRFPTLFSSEEAKQIVALFERAFVHRPYGEAGRFELLKMSELQPIEKRVLVEKHLISPHLAEDSPFGACLLSENEEISIMINEEDHIRIQCLFPGLQLAEALEAASELDDWIEGHVNYAFDERLGYLTSCPTNVGTGLRASVMMHLPALVLTQQINRIIPAINQLGLVVRGTYGEGSEALGNIFQISNQITLGKSEEDIVADLHTIVEQLIAQERAARQALVKTLGIQLEDKVFRSYGILANCRVIDSKEAAQCLSDVRLGIDLGYIKNVSRNILNELMILTQPGFLQQYAGGVLRPEERDVRRAALIRERLRMETRRKMEGDER","length":363,"molWeight":40853,"crc64":"DE55B7DE22920D45","md5":"8EE6E71FC722C7FD824623E1C1DDA458"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Motif":1,"Binding site":5,"Mutagenesis":8,"Helix":18,"Turn":4,"Beta strand":8},"uniParcId":"UPI0004AC3F54"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P11961","uniProtkbId":"ODP2_GEOSE","entryAudit":{"firstPublicDate":"1989-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":158,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex"},"ecNumbers":[{"value":"2.3.1.12"}]},"alternativeNames":[{"fullName":{"value":"Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex"}},{"fullName":{"value":"E2"}}]},"genes":[{"geneName":{"value":"pdhC"}}],"comments":[{"texts":[{"value":"The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA = N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17017"},{"database":"Rhea","id":"RHEA-COMP:10475"},{"database":"Rhea","id":"RHEA-COMP:10478"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:83100"},{"database":"ChEBI","id":"CHEBI:83111"}],"ecNumber":"2.3.1.12"}},{"commentType":"COFACTOR","cofactors":[{"name":"(R)-lipoate","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:83088"}}],"note":{"texts":[{"value":"Binds 1 lipoyl cofactor covalently."}]}},{"texts":[{"value":"Forms a 60-polypeptide structural core with icosahedral symmetry"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P11961","intActId":"EBI-1040691"},"interactantTwo":{"uniProtKBAccession":"P11959","geneName":"pdhD","intActId":"EBI-9021392"},"numberOfExperiments":3,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the 2-oxoacid dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3421911"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex","featureId":"PRO_0000162273"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Lipoyl-binding","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01066"}]},{"type":"Domain","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Peripheral subunit-binding (PSBD)","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01170"}]},{"type":"Region","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Modified residue","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"N6-lipoyllysine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01066"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8445635"}]},{"type":"Beta strand","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Beta strand","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Beta strand","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Beta strand","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Beta strand","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Beta strand","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Beta strand","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LAB"}]},{"type":"Helix","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1W85"}]},{"type":"Turn","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1W85"}]},{"type":"Helix","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1W85"}]},{"type":"Helix","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1W85"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0450","category":"Domain","name":"Lipoyl"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"2200674","citationType":"journal article","authors":["Hawkins C.F.","Borges A.","Perham R.N."],"citationCrossReferences":[{"database":"PubMed","id":"2200674"},{"database":"DOI","id":"10.1111/j.1432-1033.1990.tb19128.x"}],"title":"Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.","publicationDate":"1990","journal":"Eur. J. Biochem.","firstPage":"337","lastPage":"346","volume":"191"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"3421911","citationType":"journal article","authors":["Packman L.C.","Borges A.","Perham R.N."],"citationCrossReferences":[{"database":"PubMed","id":"3421911"},{"database":"DOI","id":"10.1042/bj2520079"}],"title":"Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus.","publicationDate":"1988","journal":"Biochem. J.","firstPage":"79","lastPage":"86","volume":"252"},"referencePositions":["PROTEIN SEQUENCE OF 2-201"]},{"referenceNumber":3,"citation":{"id":"1915365","citationType":"journal article","authors":["Dardel F.","Laue E.D.","Perham R.N."],"citationCrossReferences":[{"database":"PubMed","id":"1915365"},{"database":"DOI","id":"10.1111/j.1432-1033.1991.tb16275.x"}],"title":"Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.","publicationDate":"1991","journal":"Eur. J. Biochem.","firstPage":"203","lastPage":"209","volume":"201"},"referencePositions":["STRUCTURE BY NMR OF 1-86"]},{"referenceNumber":4,"citation":{"id":"8445635","citationType":"journal article","authors":["Dardel F.","Davis A.L.","Laue E.D.","Perham R.N."],"citationCrossReferences":[{"database":"PubMed","id":"8445635"},{"database":"DOI","id":"10.1006/jmbi.1993.1103"}],"title":"Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.","publicationDate":"1993","journal":"J. Mol. Biol.","firstPage":"1037","lastPage":"1048","volume":"229"},"referencePositions":["STRUCTURE BY NMR OF 1-86","LIPOYLATION AT LYS-43"]},{"referenceNumber":5,"citation":{"id":"8450544","citationType":"journal article","authors":["Kalia Y.N.","Brocklehurst S.M.","Hipps D.S.","Appella E.","Sakaguchi K.","Perham R.N."],"citationCrossReferences":[{"database":"PubMed","id":"8450544"},{"database":"DOI","id":"10.1006/jmbi.1993.1145"}],"title":"The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.","publicationDate":"1993","journal":"J. Mol. Biol.","firstPage":"323","lastPage":"341","volume":"230"},"referencePositions":["STRUCTURE BY NMR OF 129-171"]},{"referenceNumber":6,"citation":{"id":"8805537","citationType":"journal article","authors":["Mande S.S.","Sarfaty S.","Allen M.D.","Perham R.N.","Hol W.G.J."],"citationCrossReferences":[{"database":"PubMed","id":"8805537"},{"database":"DOI","id":"10.1016/s0969-2126(96)00032-9"}],"title":"Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.","publicationDate":"1996","journal":"Structure","firstPage":"277","lastPage":"286","volume":"4"},"referencePositions":["X-RAY CRYSTALLOGRAPHY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X53560","properties":[{"key":"ProteinId","value":"CAA37630.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S10799","properties":[{"key":"EntryName","value":"S14426"}]},{"database":"RefSeq","id":"WP_033016211.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000001.1"}]},{"database":"PDB","id":"1B5S","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"4.40 A"},{"key":"Chains","value":"A/B/C/D/E=185-426"}]},{"database":"PDB","id":"1EBD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"C=130-170"}]},{"database":"PDB","id":"1LAB","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=2-81"}]},{"database":"PDB","id":"1LAC","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=2-81"}]},{"database":"PDB","id":"1W3D","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=118-171"}]},{"database":"PDB","id":"1W4E","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=124-170"}]},{"database":"PDB","id":"1W4F","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=124-170"}]},{"database":"PDB","id":"1W4G","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=124-170"}]},{"database":"PDB","id":"1W85","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"I/J=123-171"}]},{"database":"PDB","id":"1W88","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"I/J=123-171"}]},{"database":"PDB","id":"2PDD","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=129-171"}]},{"database":"PDB","id":"2PDE","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=129-171"}]},{"database":"PDB","id":"3DUF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"I/J=1-428"}]},{"database":"PDB","id":"3DV0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"I/J=1-428"}]},{"database":"PDB","id":"3DVA","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.35 A"},{"key":"Chains","value":"I/J=1-428"}]},{"database":"PDB","id":"9UKZ","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"4.20 A"},{"key":"Chains","value":"A/B/C=185-426"}]},{"database":"AlphaFoldDB","id":"P11961","properties":[{"key":"Description","value":"-"}]},{"database":"BMRB","id":"P11961","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"P11961","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P11961","properties":[{"key":"Description","value":"-"}]},{"database":"DIP","id":"DIP-6156N","properties":[{"key":"Description","value":"-"}]},{"database":"IntAct","id":"P11961","properties":[{"key":"Interactions","value":"3"}]},{"database":"GeneID","id":"89611723","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9805770at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.3.1.12","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"P11961","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004742","properties":[{"key":"GoTerm","value":"F:dihydrolipoyllysine-residue acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0031405","properties":[{"key":"GoTerm","value":"F:lipoic acid binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06849","properties":[{"key":"EntryName","value":"lipoyl_domain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.50.100:FF:000055","properties":[{"key":"EntryName","value":"Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.559.10:FF:000007","properties":[{"key":"EntryName","value":"Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"4.10.320.10:FF:000011","properties":[{"key":"EntryName","value":"Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.559.10","properties":[{"key":"EntryName","value":"Chloramphenicol acetyltransferase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"4.10.320.10","properties":[{"key":"EntryName","value":"E3-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003016","properties":[{"key":"EntryName","value":"2-oxoA_DH_lipoyl-BS"}]},{"database":"InterPro","id":"IPR001078","properties":[{"key":"EntryName","value":"2-oxoacid_DH_actylTfrase"}]},{"database":"InterPro","id":"IPR050743","properties":[{"key":"EntryName","value":"2-oxoacid_DH_E2_comp"}]},{"database":"InterPro","id":"IPR000089","properties":[{"key":"EntryName","value":"Biotin_lipoyl"}]},{"database":"InterPro","id":"IPR023213","properties":[{"key":"EntryName","value":"CAT-like_dom_sf"}]},{"database":"InterPro","id":"IPR036625","properties":[{"key":"EntryName","value":"E3-bd_dom_sf"}]},{"database":"InterPro","id":"IPR004167","properties":[{"key":"EntryName","value":"PSBD"}]},{"database":"InterPro","id":"IPR011053","properties":[{"key":"EntryName","value":"Single_hybrid_motif"}]},{"database":"PANTHER","id":"PTHR43178","properties":[{"key":"EntryName","value":"DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43178:SF5","properties":[{"key":"EntryName","value":"LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00198","properties":[{"key":"EntryName","value":"2-oxoacid_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00364","properties":[{"key":"EntryName","value":"Biotin_lipoyl"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02817","properties":[{"key":"EntryName","value":"E3_binding"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52777","properties":[{"key":"EntryName","value":"CoA-dependent acyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47005","properties":[{"key":"EntryName","value":"Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51230","properties":[{"key":"EntryName","value":"Single hybrid motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50968","properties":[{"key":"EntryName","value":"BIOTINYL_LIPOYL"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00189","properties":[{"key":"EntryName","value":"LIPOYL"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51826","properties":[{"key":"EntryName","value":"PSBD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLDAPGYENMTFKGQEQEEAKKEEKTETVSKEEKVDAVAPNAPAAEAEAGPNRRVIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGAKPAPAAAEEKAAPAAAKPATTEGEFPETREKMSGIRRAIAKAMVHSKHTAPHVTLMDEADVTKLVAHRKKFKAIAAEKGIKLTFLPYVVKALVSALREYPVLNTSIDDETEEIIQKHYYNIGIAADTDRGLLVPVIKHADRKPIFALAQEINELAEKARDGKLTPGEMKGASCTITNIGSAGGQWFTPVINHPEVAILGIGRIAEKPIVRDGEIVAAPMLALSLSFDHRMIDGATAQKALNHIKRLLSDPELLLMEA","length":428,"molWeight":46326,"crc64":"2600CD150261ACB0","md5":"EC121B2E15F7D0B8D171446A6F923097"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"INTERACTION":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Domain":2,"Region":2,"Compositional bias":3,"Active site":1,"Modified residue":1,"Beta strand":7,"Helix":3,"Turn":1},"uniParcId":"UPI000016E908"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P56255","uniProtkbId":"PCRA_GEOSE","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-07-15","entryVersion":115,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9592155"}],"value":"ATP-dependent DNA helicase PcrA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA 3'-5' helicase PcrA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9592155"}],"value":"pcrA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}],"value":"3'-5' DNA helicase with single-stranded (ss)DNA-stimulated ATPase activity (PubMed:9592155, PubMed:10388562, PubMed:10454638). A broad specificity DNA-dependent NTPase, couples the hydrolysis of natural (d)NTPs to DNA unwinding (PubMed:9592155). It is a 3'-5' helicase but at high protein concentrations will also displace a substrate with a 5'-tail (PubMed:9592155). The preferred substrate is duplex DNA with a 3'-ss-extension (PubMed:9592155)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.35,"unit":"mM","substrate":"ATP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"constant":56.0,"unit":"uM","substrate":"ATP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}]},{"constant":225.0,"unit":"uM","substrate":"ATP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}]},{"constant":0.29,"unit":"mM","substrate":"dATP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"constant":0.18,"unit":"mM","substrate":"CTP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"constant":0.3,"unit":"mM","substrate":"GTP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"constant":0.25,"unit":"mM","substrate":"dGTP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"constant":0.68,"unit":"mM","substrate":"dTTP (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"constant":0.11,"unit":"mM","substrate":"1,N6-ethenoadenosine 5'-triphosphate (for hydrolysis activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}],"value":"kcat is 19 sec(-1) with ATP as substrate, and varies from 3-40 sec(-1) depending on the (d)NTP. In the absence of single-stranded (ss)DNA, kcat decreases 400-fold with ATP as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10199404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8934527"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10199404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"value":"There are significant domain movements between the substrate and product complex"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the helicase family. UvrD subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":724,"modifier":"EXACT"}},"description":"ATP-dependent DNA helicase PcrA","featureId":"PRO_0000102050"},{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00560"}]},{"type":"Domain","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":569,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00617"}]},{"type":"Region","location":{"start":{"value":652,"modifier":"EXACT"},"end":{"value":674,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10199404"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10199404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":569,"modifier":"EXACT"},"end":{"value":569,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":571,"modifier":"EXACT"},"end":{"value":571,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":610,"modifier":"EXACT"},"end":{"value":610,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10199404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"ATP gamma phosphate sensor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}]},{"type":"Mutagenesis","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Significant decrease in helicase activity, 12-fold decrease in ATP-binding, 30-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"Significant decrease in helicase activity, 1250-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Significant decrease in helicase activity, 180-830-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A","N"]}},{"type":"Mutagenesis","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Significant decrease in helicase activity, 4-fold decrease in ATP-binding, 70-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Severely reduced helicase activity, reduced kcat for ATP hydrolysis, greatly reduced ATP binding, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Severely reduced helicase activity, reduced kcat for ATP hydrolysis, slightly reduced ATP binding, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Considerably reduced helicase activity, reduced kcat for ATP hydrolysis, slightly reduced ATP binding, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Reduced helicase activity, reduced kcat for ATP hydrolysis, wild-type ATP binding, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["R","K"]}},{"type":"Mutagenesis","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"300-fold decrease in helicase activity, severely decreased ssDNA-binding, KM for ATP unchanged, ATP hydrolysis requires 200-fold more ssDNA for stimulation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"90-fold decrease in helicase activity, slightly decreased ssDNA-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"Decrease in helicase activity, 19-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"Decrease in helicase activity, 4-fold decrease in ATP-binding, 12-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":610,"modifier":"EXACT"},"end":{"value":610,"modifier":"EXACT"}},"description":"Significant decrease in helicase activity, 38-fold decrease in kcat for ATP hydrolysis, binds ssDNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Helix","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Helix","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Helix","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Beta strand","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Beta strand","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Turn","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Turn","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Turn","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":446,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":454,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":462,"modifier":"EXACT"},"end":{"value":474,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":503,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":531,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":538,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":544,"modifier":"EXACT"},"end":{"value":546,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2PJR"}]},{"type":"Beta strand","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":563,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":564,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":572,"modifier":"EXACT"},"end":{"value":577,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Turn","location":{"start":{"value":584,"modifier":"EXACT"},"end":{"value":586,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":588,"modifier":"EXACT"},"end":{"value":591,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":594,"modifier":"EXACT"},"end":{"value":608,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":611,"modifier":"EXACT"},"end":{"value":625,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":628,"modifier":"EXACT"},"end":{"value":630,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":636,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Helix","location":{"start":{"value":643,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":646,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PJR"}]},{"type":"Beta strand","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":681,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Turn","location":{"start":{"value":682,"modifier":"EXACT"},"end":{"value":684,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Beta strand","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":694,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Helix","location":{"start":{"value":696,"modifier":"EXACT"},"end":{"value":698,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Beta strand","location":{"start":{"value":700,"modifier":"EXACT"},"end":{"value":705,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Turn","location":{"start":{"value":706,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Beta strand","location":{"start":{"value":710,"modifier":"EXACT"},"end":{"value":716,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]},{"type":"Beta strand","location":{"start":{"value":720,"modifier":"EXACT"},"end":{"value":723,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5DMA"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"9592155","citationType":"journal article","authors":["Bird L.E.","Brannigan J.A.","Subramanya H.S.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"9592155"},{"database":"DOI","id":"10.1093/nar/26.11.2686"}],"title":"Characterisation of Bacillus stearothermophilus PcrA helicase: evidence against an active rolling mechanism.","publicationDate":"1998","journal":"Nucleic Acids Res.","firstPage":"2686","lastPage":"2693","volume":"26"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","DNA-BINDING"]},{"referenceNumber":2,"citation":{"id":"10454638","citationType":"journal article","authors":["Dillingham M.S.","Soultanas P.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"10454638"},{"database":"DOI","id":"10.1093/nar/27.16.3310"}],"title":"Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation.","publicationDate":"1999","journal":"Nucleic Acids Res.","firstPage":"3310","lastPage":"3317","volume":"27"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SITE","MUTAGENESIS OF GLN-254; TRP-259 AND ARG-260"]},{"referenceNumber":3,"citation":{"id":"8934527","citationType":"journal article","authors":["Subramanya H.S.","Bird L.E.","Brannigan J.A.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"8934527"},{"database":"DOI","id":"10.1038/384379a0"}],"title":"Crystal structure of a DExx box DNA helicase.","publicationDate":"1996","journal":"Nature","firstPage":"379","lastPage":"383","volume":"384"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","SUBUNIT"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PJR"}]},{"referenceNumber":4,"citation":{"id":"10199404","citationType":"journal article","authors":["Velankar S.S.","Soultanas P.","Dillingham M.S.","Subramanya H.S.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"10199404"},{"database":"DOI","id":"10.1016/s0092-8674(00)80716-3"}],"title":"Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism.","publicationDate":"1999","journal":"Cell","firstPage":"75","lastPage":"84","volume":"97"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATP AND DNA","SUBUNIT","DOMAIN","DNA-BINDING"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"2PJR"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3PJR"}]},{"referenceNumber":5,"citation":{"id":"10388562","citationType":"journal article","authors":["Soultanas P.","Dillingham M.S.","Velankar S.S.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"10388562"},{"database":"DOI","id":"10.1006/jmbi.1999.2873"}],"title":"DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase.","publicationDate":"1999","journal":"J. Mol. Biol.","firstPage":"137","lastPage":"148","volume":"290"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATP AND MG(2+)","FUNCTION","CATALYTIC ACTIVITY","SUBUNIT","DOMAIN","DNA-BINDING","MUTAGENESIS OF LYS-37; THR-38; ASP-223; GLU-224; ARG-287; LYS-568 AND ARG-610"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHG"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QHH"}]}],"uniProtKBCrossReferences":[{"database":"PDB","id":"1PJR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A=1-724"}]},{"database":"PDB","id":"1QHG","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A=1-724"}]},{"database":"PDB","id":"1QHH","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A=1-167, B=168-440, C=441-555, D=556-724"}]},{"database":"PDB","id":"2PJR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.90 A"},{"key":"Chains","value":"A/F=1-548, B/G=556-650"}]},{"database":"PDB","id":"3PJR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.30 A"},{"key":"Chains","value":"A=1-724"}]},{"database":"PDB","id":"5DMA","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.53 A"},{"key":"Chains","value":"A=673-724"}]},{"database":"AlphaFoldDB","id":"P56255","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"P56255","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P56255","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"5.6.2.4","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"P56255","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033202","properties":[{"key":"GoTerm","value":"C:DNA helicase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388562"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10454638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9592155"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000725","properties":[{"key":"GoTerm","value":"P:recombinational repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009314","properties":[{"key":"GoTerm","value":"P:response to radiation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd17932","properties":[{"key":"EntryName","value":"DEXQc_UvrD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18807","properties":[{"key":"EntryName","value":"SF1_C_UvrD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.160:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.486.10:FF:000003","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.160","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.486.10","properties":[{"key":"EntryName","value":"PCRA, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005751","properties":[{"key":"EntryName","value":"ATP-dep_DNA_helicase_PcrA"}]},{"database":"InterPro","id":"IPR013986","properties":[{"key":"EntryName","value":"DExx_box_DNA_helicase_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR000212","properties":[{"key":"EntryName","value":"UvrD-like"}]},{"database":"InterPro","id":"IPR014016","properties":[{"key":"EntryName","value":"UvrD-like_ATP-bd"}]},{"database":"InterPro","id":"IPR014017","properties":[{"key":"EntryName","value":"UvrD-like_C"}]},{"database":"NCBIfam","id":"TIGR01073","properties":[{"key":"EntryName","value":"pcrA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070:SF2","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE SRS2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070","properties":[{"key":"EntryName","value":"UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21196","properties":[{"key":"EntryName","value":"PcrA_UvrD_tudor"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00580","properties":[{"key":"EntryName","value":"UvrD-helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13361","properties":[{"key":"EntryName","value":"UvrD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51198","properties":[{"key":"EntryName","value":"UVRD_HELICASE_ATP_BIND"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51217","properties":[{"key":"EntryName","value":"UVRD_HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFLSEQLLAHLNKEQQEAVRTTEGPLLIMAGAGSGKTRVLTHRIAYLMAEKHVAPWNILAITFTNKAAREMRERVQSLLGGAAEDVWISTFHSMCVRILRRDIDRIGINRNFSILDPTDQLSVMKTILKEKNIDPKKFEPRTILGTISAAKNELLPPEQFAKRASTYYEKVVSDVYQEYQQRLLRNHSLDFDDLIMTTIQLFDRVPDVLHYYQYKFQYIHIDEYQDTNRAQYTLVKKLAERFQNICAVGDADQSIYRWRGADIQNILSFERDYPNAKVILLEQNYRSTKRILQAANEVIEHNVNRKPKRIWTENPEGKPILYYEAMNEADEAQFVAGRIREAVERGERRYRDFAVLYRTNAQSRVMEEMLLKANIPYQIVGGLKFYDRKEIKDILAYLRVIANPDDDLSLLRIINVPKRGIGASTIDKLVRYAADHELSLFEALGELEMIGLGAKAAGALAAFRSQLEQWTQLQEYVSVTELVEEVLDKSGYREMLKAERTIEAQSRLENLDEFLSVTKHFENVSDDKSLIAFLTDLALISDLDELDGTEQAAEGDAVMLMTLHAAKGLEFPVVFLIGMEEGIFPHNRSLEDDDEMEEERRLAYVGITRAEEELVLTSAQMRTLFGNIQMDPPSRFLNEIPAHLLETASRRQAGASRPAVSRPQASGAVGSWKVGDRANHRKWGIGTVVSVRGGGDDQELDIAFPSPIGIKRLLAKFAPIEKV","length":724,"molWeight":82488,"crc64":"6D20CA468BFB4291","md5":"FF3A92F01B3FAF58541878580FFA1E2A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Region":1,"Binding site":16,"Site":1,"Mutagenesis":13,"Helix":41,"Beta strand":25,"Turn":13},"uniParcId":"UPI0000112974"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9ALJ4","uniProtkbId":"AGAA_GEOSE","entryAudit":{"firstPublicDate":"2017-04-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-06-01","entryVersion":81,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG49420.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG49420.1"}],"value":"Alpha-galactosidase AgaA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16511274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"3.2.1.22"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG49420.1"}],"value":"agaA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"value":"Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.","ecNumber":"3.2.1.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16511274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"Not inhibited by D-galactose or sucrose (Ref.1). Inhibited by pharmaceutical drug 1-deoxygalactonojirimycin (PubMed:23012371)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.21,"unit":"mM","substrate":"p-nitrophenyl-alpha-galactopyranoside (at 25 degrees Celsius and pH 6.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}]},{"constant":3.8,"unit":"mM","substrate":"raffinose (at 25 degrees Celsius and pH 6.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"value":"kcat is 105 sec(-1) for p-nitrophenyl-alpha-galactopyranoside (at 25 degrees Celsius and pH 6.5). kcat is 180 sec(-1) for raffinose (at 25 degrees Celsius and pH 6.5)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"Optimum pH is 6.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"Optimum temperature is 65 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"G1UB44"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"Has properties that make it suitable for elimination of D-raffinose from low green syrup in sugar manufacturing process from beets in order to improve the yield of sucrose"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 36 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":729,"modifier":"EXACT"}},"description":"Alpha-galactosidase AgaA","featureId":"PRO_0000439585"},{"type":"Active site","location":{"start":{"value":478,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}]},{"type":"Active site","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}]},{"type":"Binding site","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":476,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":526,"modifier":"EXACT"},"end":{"value":526,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNT"}],"ligand":{"name":"substrate"}},{"type":"Mutagenesis","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Very strongly reduced hydrolytic efficiency against raffinose, but displays medium level of transglycosylation activity compared to none with wild-type enzyme.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Strongly reduced hydrolytic efficiency against raffinose, but displays high level of transglycosylation activity compared to none with wild-type enzyme.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["F","S"]}},{"type":"Mutagenesis","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Very strongly reduced hydrolytic efficiency against raffinose, but displays low level of transglycosylation activity compared to none with wild-type enzyme.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":478,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23012371"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Beta strand","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNR"}]},{"type":"Beta strand","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNR"}]},{"type":"Beta strand","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNP"}]},{"type":"Turn","location":{"start":{"value":387,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":444,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":446,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":535,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":541,"modifier":"EXACT"},"end":{"value":545,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":554,"modifier":"EXACT"},"end":{"value":562,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":563,"modifier":"EXACT"},"end":{"value":565,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":570,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":571,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":581,"modifier":"EXACT"},"end":{"value":583,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":589,"modifier":"EXACT"},"end":{"value":596,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":599,"modifier":"EXACT"},"end":{"value":603,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":607,"modifier":"EXACT"},"end":{"value":609,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":612,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":635,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":643,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":646,"modifier":"EXACT"},"end":{"value":654,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":658,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":677,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":688,"modifier":"EXACT"},"end":{"value":692,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Turn","location":{"start":{"value":693,"modifier":"EXACT"},"end":{"value":695,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":696,"modifier":"EXACT"},"end":{"value":699,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Helix","location":{"start":{"value":700,"modifier":"EXACT"},"end":{"value":705,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]},{"type":"Beta strand","location":{"start":{"value":708,"modifier":"EXACT"},"end":{"value":710,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNT"}]},{"type":"Beta strand","location":{"start":{"value":715,"modifier":"EXACT"},"end":{"value":726,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4FNS"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8K8H57UURMIP2","citationType":"journal article","authors":["Ganter C.","Boeck A.","Buckel P.","Mattes R."],"title":"Production of thermostable, recombinant alpha-galactosidase suitable for raffinose elimination from sugar beet syrup.","publicationDate":"1988","journal":"J. Biotechnol.","firstPage":"301","lastPage":"310","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","BIOTECHNOLOGY"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG49420.1"}],"value":"KVE39","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG49420.1"}]},{"referenceNumber":2,"citation":{"id":"16511274","citationType":"journal article","authors":["Foucault M.","Watzlawick H.","Mattes R.","Haser R.","Gouet P."],"citationCrossReferences":[{"database":"PubMed","id":"16511274"},{"database":"DOI","id":"10.1107/s1744309105042582"}],"title":"Crystallization and preliminary X-ray diffraction studies of two thermostable alpha-galactosidases from glycoside hydrolase family 36.","publicationDate":"2006","journal":"Acta Crystallogr. F","firstPage":"100","lastPage":"103","volume":"62"},"referencePositions":["CRYSTALLIZATION OF MUTANT GLU-355","CATALYTIC ACTIVITY"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16511274"}],"value":"KVE39","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"23012371","citationType":"journal article","authors":["Merceron R.","Foucault M.","Haser R.","Mattes R.","Watzlawick H.","Gouet P."],"citationCrossReferences":[{"database":"PubMed","id":"23012371"},{"database":"DOI","id":"10.1074/jbc.m112.394114"}],"title":"The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"39642","lastPage":"39652","volume":"287"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF SUBSTRATE-FREE WILD-TYPE AND MUTANT GLU-355 AND IN COMPLEX WITH RAFFINOSE; STACHYOSE AND INHIBITOR","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","ACTIVE SITE","MUTAGENESIS OF TRP-336; ASP-478 AND ASP-548"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNR"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4FNS"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY013286","properties":[{"key":"ProteinId","value":"AAG49420.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"4FNP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A/B/C/D=1-729"}]},{"database":"PDB","id":"4FNR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.20 A"},{"key":"Chains","value":"A/B/C/D=1-729"}]},{"database":"PDB","id":"4FNS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B/C/D=1-729"}]},{"database":"PDB","id":"4FNT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B/C/D=1-729"}]},{"database":"PDB","id":"4FNU","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.60 A"},{"key":"Chains","value":"A/B/C/D=1-729"}]},{"database":"AlphaFoldDB","id":"Q9ALJ4","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q9ALJ4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9ALJ4","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH36","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 36"}]},{"database":"BRENDA","id":"3.2.1.22","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"Q9ALJ4","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004557","properties":[{"key":"GoTerm","value":"F:alpha-galactosidase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"16511274"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23012371"}]},{"database":"GO","id":"GO:0051289","properties":[{"key":"GoTerm","value":"P:protein homotetramerization"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0034484","properties":[{"key":"GoTerm","value":"P:raffinose catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23012371"}]},{"database":"GO","id":"GO:0033531","properties":[{"key":"GoTerm","value":"P:stachyose metabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23012371"}]},{"database":"CDD","id":"cd14791","properties":[{"key":"EntryName","value":"GH36"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000118","properties":[{"key":"EntryName","value":"Alpha-galactosidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.70.98.60:FF:000006","properties":[{"key":"EntryName","value":"Alpha-galactosidase AgaA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.98.60","properties":[{"key":"EntryName","value":"alpha-galactosidase from lactobacil brevis"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1180","properties":[{"key":"EntryName","value":"Golgi alpha-mannosidase II"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR038417","properties":[{"key":"EntryName","value":"Alpga-gal_N_sf"}]},{"database":"InterPro","id":"IPR050985","properties":[{"key":"EntryName","value":"Alpha-glycosidase_related"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR000111","properties":[{"key":"EntryName","value":"Glyco_hydro_27/36_CS"}]},{"database":"InterPro","id":"IPR002252","properties":[{"key":"EntryName","value":"Glyco_hydro_36"}]},{"database":"InterPro","id":"IPR031705","properties":[{"key":"EntryName","value":"Glyco_hydro_36_C"}]},{"database":"InterPro","id":"IPR031704","properties":[{"key":"EntryName","value":"Glyco_hydro_36_N"}]},{"database":"InterPro","id":"IPR013780","properties":[{"key":"EntryName","value":"Glyco_hydro_b"}]},{"database":"PANTHER","id":"PTHR43053:SF3","properties":[{"key":"EntryName","value":"ALPHA-GALACTOSIDASE C-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43053","properties":[{"key":"EntryName","value":"GLYCOSIDASE FAMILY 31"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16874","properties":[{"key":"EntryName","value":"Glyco_hydro_36C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16875","properties":[{"key":"EntryName","value":"Glyco_hydro_36N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02065","properties":[{"key":"EntryName","value":"Melibiase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005536","properties":[{"key":"EntryName","value":"Agal"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00743","properties":[{"key":"EntryName","value":"GLHYDRLASE36"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00512","properties":[{"key":"EntryName","value":"ALPHA_GALACTOSIDASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVAYNPQTKQFHLRAGKASYVMQLFRSGYLAHVYWGKAVRDVRGARAFPRLDRAFSPNPDPSDRTFSLDTLLQEYPAYGNTDFRAPAYQVQLENGSTVTDLRYKTHRIYKGKPRLNGLPATYVEHEQEAETLEIVLGDALIGLEVTLQYTAYEKWNVITRSARFENKGGERLKLLRALSMSVDFPTADYDWIHLPGAWGRERWIERRPLVTGVQAAESRRGASSHQQNPFIALVAKNADEHQGEVYGFSFVYSGNFLAQIEVDQFGTARVSMGINPFDFTWLLQPGESFQTPEVVMVYSDQGLNGMSQTYHELYRTRLARGAFRDRERPILINNWEATYFDFNEEKIVNIARTAAELGIELVVLDDGWFGERDDDRRSLGDWIVNRRKLPNGLDGLAKQVNELGLQFGLWVEPEMVSPNSELYRKHPDWCLHVPNRPRSEGRNQLVLDYSREDVCDYIIETISNVLASAPITYVKWDMNRHMTEIGSSALPPERQRETAHRYMLGLYRVMDEITSRFPHILFESCSGGGGRFDPGMLYYMPQTWTSDNTDAVSRLKIQYGTSLVYPISAMGAHVSAVPNHQVGRVASLKTRGHVAMSGNFGYELDITKLTETEKQMMKQQVAFYKDVRRLVQFGTFYRLLSPFEGNEAAWMFVSADRSEALVAYFRVLAEANAPLSYLRLKGLDSNQDYEIEGLGVYGGDELMYAGVALPYRSSDFISMMWRLKAVQQ","length":729,"molWeight":83211,"crc64":"6E59129E1C3502A2","md5":"77A0B9969F3FBD604F57E1EF1E577398"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"BIOTECHNOLOGY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":7,"Mutagenesis":5,"Beta strand":47,"Turn":9,"Helix":20},"uniParcId":"UPI00000BA828"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9S467","secondaryAccessions":["Q335M1"],"uniProtkbId":"ARAA_GEOSE","entryAudit":{"firstPublicDate":"2002-01-23","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2002-01-23","entryVersion":83,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"L-arabinose isomerase"},"ecNumbers":[{"value":"5.3.1.4"}]}},"genes":[{"geneName":{"value":"araA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"}],"value":"Catalyzes the conversion of L-arabinose to L-ribulose. In vitro, converts D-galactose into D-tagatose"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-L-arabinopyranose = L-ribulose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14821"},{"database":"ChEBI","id":"CHEBI:16880"},{"database":"ChEBI","id":"CHEBI:40886"}],"ecNumber":"5.3.1.4"}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"value":"Binds 1 Mn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"}],"value":"Inhibited by copper"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":41.8,"unit":"umol/min/mg","enzyme":"enzyme with L-arabinose as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}]},{"velocity":8.9,"unit":"umol/min/mg","enzyme":"enzyme with D-galactose as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}]}],"michaelisConstants":[{"constant":28.0,"unit":"mM","substrate":"L-arabinose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}]},{"constant":57.0,"unit":"mM","substrate":"D-galactose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"value":"Optimum pH is 7.5-8.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"value":"Optimum temperature is 80 degrees Celsius."}]}},{"texts":[{"value":"Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16386851"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the arabinose isomerase family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAD45718.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"L-arabinose isomerase","featureId":"PRO_0000198381"},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":447,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Mutagenesis","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Increases KM for L-arabinose.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":447,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17337581"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"MMI","alternativeSequences":["RIM"]}},{"type":"Sequence conflict","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"LNQ","alternativeSequences":["WNR"]}},{"type":"Sequence conflict","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["F"]}},{"type":"Sequence conflict","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"LEP","alternativeSequences":["FEL"]}},{"type":"Sequence conflict","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"M","alternativeSequences":["L"]}},{"type":"Sequence conflict","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Sequence conflict","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":487,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"in Ref. 2; CAI29261","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}}],"keywords":[{"id":"KW-0054","category":"Biological process","name":"Arabinose catabolism"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-2KM2UPTEN2IHC","citationType":"submission","authors":["Gilead-Gropper S.","Shoham Y."],"title":"The L-arabinose utilization gene cluster from Bacillus stearothermophilus T-6.","publicationDate":"JUN-1999","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"16386851","citationType":"journal article","authors":["Rhimi M.","Bejar S."],"citationCrossReferences":[{"database":"PubMed","id":"16386851"},{"database":"DOI","id":"10.1016/j.bbagen.2005.11.007"}],"title":"Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive L-arabinose isomerase from the Bacillus stearothermophilus US100 strain.","publicationDate":"2006","journal":"Biochim. Biophys. Acta","firstPage":"191","lastPage":"199","volume":"1760"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","SUBUNIT","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"US100","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"17337581","citationType":"journal article","authors":["Rhimi M.","Juy M.","Aghajari N.","Haser R.","Bejar S."],"citationCrossReferences":[{"database":"PubMed","id":"17337581"},{"database":"DOI","id":"10.1128/jb.01826-06"}],"title":"Probing the essential catalytic residues and substrate affinity in the thermoactive Bacillus stearothermophilus US100 L-arabinose isomerase by site-directed mutagenesis.","publicationDate":"2007","journal":"J. Bacteriol.","firstPage":"3556","lastPage":"3563","volume":"189"},"referencePositions":["COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","IDENTIFICATION BY MASS SPECTROMETRY","MUTAGENESIS OF PHE-279; GLU-306; GLU-331; HIS-348 AND HIS-447"],"referenceComments":[{"value":"US100","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF160811","properties":[{"key":"ProteinId","value":"AAD45718.1"},{"key":"Status","value":"ALT_INIT"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AJ866972","properties":[{"key":"ProteinId","value":"CAI29261.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9S467","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9S467","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"5.3.1.4","properties":[{"key":"OrganismId","value":"623"}]},{"database":"SABIO-RK","id":"Q9S467","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00145","properties":[{"key":"RectionId","value":"UER00565"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008733","properties":[{"key":"GoTerm","value":"F:L-arabinose isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005996","properties":[{"key":"GoTerm","value":"P:monosaccharide metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03557","properties":[{"key":"EntryName","value":"L-arabinose_isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10940","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00519","properties":[{"key":"EntryName","value":"Arabinose_Isome"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024664","properties":[{"key":"EntryName","value":"Ara_Isoase_C"}]},{"database":"InterPro","id":"IPR055390","properties":[{"key":"EntryName","value":"AraA_central"}]},{"database":"InterPro","id":"IPR055389","properties":[{"key":"EntryName","value":"AraA_N"}]},{"database":"InterPro","id":"IPR038583","properties":[{"key":"EntryName","value":"AraA_N_sf"}]},{"database":"InterPro","id":"IPR004216","properties":[{"key":"EntryName","value":"Fuc/Ara_isomerase_C"}]},{"database":"InterPro","id":"IPR009015","properties":[{"key":"EntryName","value":"Fucose_isomerase_N/cen_sf"}]},{"database":"InterPro","id":"IPR003762","properties":[{"key":"EntryName","value":"Lara_isomerase"}]},{"database":"NCBIfam","id":"NF002795","properties":[{"key":"EntryName","value":"araA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR38464","properties":[{"key":"EntryName","value":"L-ARABINOSE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR38464:SF1","properties":[{"key":"EntryName","value":"L-ARABINOSE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24856","properties":[{"key":"EntryName","value":"AraA_central"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02610","properties":[{"key":"EntryName","value":"AraA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11762","properties":[{"key":"EntryName","value":"Arabinose_Iso_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001478","properties":[{"key":"EntryName","value":"L-ara_isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50443","properties":[{"key":"EntryName","value":"FucI/AraA C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53743","properties":[{"key":"EntryName","value":"FucI/AraA N-terminal and middle domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLSLRPYEFWFVTGSQHLYGEEALKQVEEHSMMIVNELNQDSVFPFPLVFKSVVTTPEEIRRVCLEANASEQCAGVITWMHTFSPAKMWIGGLLELRKPLLHLHTQFNRDIPWDSIDMDFMNLNQSAHGDREYGFIGARMGVARKVVVGHWEDPEVRERLAKWMRTAVAFAESRNLKVARFGDNMREVAVTEGDKVGAQIQFGWSVNGYGIGDLVQYIRDVSEQKVNELLDEYEELYDIVPAGRQEGPVRESIREQARIELGLKAFLQDGNFTAFTTTFEDLHGMKQLPGLAVQRLMAEGYGFGGEGDWKTAALVRLMKVMADGKGTSFMEDYTYHLEPGNEMILGAHMLEVCPTIAATRPRIEVHPLSIGGKEDPARLVFDGGEGAAVNASLIDLGHRFRLIVNEVDAVKPEHDMPKLPVARILWKPRPSLRDSAEAWILAGGAHHTCFSFAVTTEQLQDFAEMAGIECVVINEHTSVSSFKNELKWNEVFWRGR","length":496,"molWeight":55957,"crc64":"3542B7B9005A0E41","md5":"96E87986D5CFDA6F48314BCFB9E57F05"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Binding site":4,"Mutagenesis":5,"Sequence conflict":8},"uniParcId":"UPI0000125D51"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00362","uniProtkbId":"G3P_GEOSE","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":163,"sequenceVersion":5},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7408868"}],"value":"Glyceraldehyde-3-phosphate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7408868"}],"value":"GAPDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P09124"}],"value":"1.2.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7408868"}],"value":"NAD-dependent glyceraldehyde-3-phosphate dehydrogenase"}}]},"genes":[{"geneName":{"value":"gap"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"}],"value":"Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = (2R)-3-phospho-glyceroyl phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10300"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57604"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"1.2.1.12","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P09124"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"193030"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3210237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9175858"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glyceraldehyde-3-phosphate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"PubMed:2684782 sequence was incorrect and retracted in PubMed:2227448"}],"commentType":"CAUTION"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7408868"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"Glyceraldehyde-3-phosphate dehydrogenase","featureId":"PRO_0000145633"},{"type":"Active site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12569100"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3210237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"D-glyceraldehyde 3-phosphate","id":"ChEBI:CHEBI:59776"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3210237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"D-glyceraldehyde 3-phosphate","id":"ChEBI:CHEBI:59776"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"D-glyceraldehyde 3-phosphate","id":"ChEBI:CHEBI:59776"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3210237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"D-glyceraldehyde 3-phosphate","id":"ChEBI:CHEBI:59776"}},{"type":"Binding site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3210237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"D-glyceraldehyde 3-phosphate","id":"ChEBI:CHEBI:59776"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3586018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Activates thiol group during catalysis","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6GIL8"}]},{"type":"Mutagenesis","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"In mutant B-S, the recognition of NAD is slightly affected; when associated with A-190 and S-191.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"alternativeSequence":{"originalSequence":"LTD","alternativeSequences":["TGG"]}},{"type":"Mutagenesis","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Loss of dehydrogenase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Possesses a low residual dehydrogenase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12569100"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"In mutant D32G-S, a strong alteration of the affinity for NAD is observed; when associated with S-191. In mutant B-S, the recognition of NAD is slightly affected; when associated with 35-T--G-37 and S-191.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"In mutant D32G-S, a strong alteration of the affinity for NAD is observed; when associated with A-190. In mutant B-S, the recognition of NAD is slightly affected; when associated with 35-T--G-37 and A-190.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9175858"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["S"]}},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Turn","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Beta strand","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]},{"type":"Helix","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3CMC"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"2684782","citationType":"journal article","authors":["Tesfay H.S.","Amelunxen R.E.","Goldberg I.D."],"citationCrossReferences":[{"database":"PubMed","id":"2684782"},{"database":"DOI","id":"10.1016/0378-1119(89)90049-8"}],"title":"Nucleotide sequences of genes encoding heat-stable and heat-labile glyceraldehyde-3-phosphate dehydrogenases; amino acid sequence and protein thermostability.","publicationDate":"1989","journal":"Gene","firstPage":"237","lastPage":"248","volume":"82"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","RETRACTED PAPER"]},{"referenceNumber":2,"citation":{"id":"2227448","citationType":"journal article","authors":["Tesfay H.S.","Amelunxen R.E.","Goldberg I.D."],"citationCrossReferences":[{"database":"PubMed","id":"2227448"},{"database":"DOI","id":"10.1016/0378-1119(90)90484-9"}],"publicationDate":"1990","journal":"Gene","firstPage":"144","lastPage":"144","volume":"94"},"referencePositions":["ERRATUM OF PUBMED:2684782","RETRACTION NOTICE OF PUBMED:2684782"]},{"referenceNumber":3,"citation":{"id":"2656407","citationType":"journal article","authors":["Branlant C.","Oster T.","Branlant G."],"citationCrossReferences":[{"database":"PubMed","id":"2656407"},{"database":"DOI","id":"10.1016/0378-1119(89)90391-0"}],"title":"Nucleotide sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the flanking DNA regions required for its expression in Escherichia coli.","publicationDate":"1989","journal":"Gene","firstPage":"145","lastPage":"155","volume":"75"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":4,"citation":{"id":"7408868","citationType":"journal article","authors":["Walker J.E.","Carne A.F.","Runswick M.J.","Bridgen J.","Harris J.I."],"citationCrossReferences":[{"database":"PubMed","id":"7408868"},{"database":"DOI","id":"10.1111/j.1432-1033.1980.tb04751.x"}],"title":"D-glyceraldehyde-3-phosphate dehydrogenase. Complete amino-acid sequence of the enzyme from Bacillus stearothermophilus.","publicationDate":"1980","journal":"Eur. J. Biochem.","firstPage":"549","lastPage":"565","volume":"108"},"referencePositions":["PROTEIN SEQUENCE OF 2-335"]},{"referenceNumber":5,"citation":{"id":"193030","citationType":"journal article","authors":["Biesecker G.","Harris J.I.","Thierry J.-C.","Walker J.E.","Wonacott A.J."],"citationCrossReferences":[{"database":"PubMed","id":"193030"},{"database":"DOI","id":"10.1038/266328a0"}],"title":"Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.","publicationDate":"1977","journal":"Nature","firstPage":"328","lastPage":"333","volume":"266"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","SUBUNIT"]},{"referenceNumber":6,"citation":{"id":"3586018","citationType":"journal article","authors":["Skarzynski T.","Moody P.C.E.","Wonacott A.J."],"citationCrossReferences":[{"database":"PubMed","id":"3586018"},{"database":"DOI","id":"10.1016/0022-2836(87)90635-8"}],"title":"Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8-A resolution.","publicationDate":"1987","journal":"J. Mol. Biol.","firstPage":"171","lastPage":"187","volume":"193"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD AND SUBSTRATE ANALOG","SUBUNIT"]},{"referenceNumber":7,"citation":{"id":"3210237","citationType":"journal article","authors":["Skarzynski T.","Wonacott A.J."],"citationCrossReferences":[{"database":"PubMed","id":"3210237"},{"database":"DOI","id":"10.1016/0022-2836(88)90130-1"}],"title":"Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus.","publicationDate":"1988","journal":"J. Mol. Biol.","firstPage":"1097","lastPage":"1118","volume":"203"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE ANALOG","SUBUNIT"]},{"referenceNumber":8,"citation":{"id":"9175858","citationType":"journal article","authors":["Didierjean C.","Rahuel-Clermont S.","Vitoux B.","Dideberg O.","Branlant G.","Aubry A."],"citationCrossReferences":[{"database":"PubMed","id":"9175858"},{"database":"DOI","id":"10.1006/jmbi.1997.0998"}],"title":"A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+.","publicationDate":"1997","journal":"J. Mol. Biol.","firstPage":"739","lastPage":"759","volume":"268"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF B-S AND D32G-S MUTANTS IN COMPLEXES WITH NAD AND SUBSTRATE ANALOG","MUTAGENESIS OF 35-LEU--ASP-37; CYS-152; LEU-190 AND PRO-191","SUBUNIT"]},{"referenceNumber":9,"citation":{"id":"12569100","citationType":"journal article","authors":["Didierjean C.","Corbier C.","Fatih M.","Favier F.","Boschi-Muller S.","Branlant G.","Aubry A."],"citationCrossReferences":[{"database":"PubMed","id":"12569100"},{"database":"DOI","id":"10.1074/jbc.m211040200"}],"title":"Crystal structure of two ternary complexes of phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus with NAD and D-glyceraldehyde 3-phosphate.","publicationDate":"2003","journal":"J. Biol. Chem.","firstPage":"12968","lastPage":"12976","volume":"278"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANT ALA-152 IN COMPLEX WITH NAD AND GLYCERALDEHYDE 3-PHOSPHATE","FUNCTION","MUTAGENESIS OF CYS-152","REACTION MECHANISM","SUBUNIT"]},{"referenceNumber":10,"citation":{"id":"18480053","citationType":"journal article","authors":["Moniot S.","Bruno S.","Vonrhein C.","Didierjean C.","Boschi-Muller S.","Vas M.","Bricogne G.","Branlant G.","Mozzarelli A.","Corbier C."],"citationCrossReferences":[{"database":"PubMed","id":"18480053"},{"database":"DOI","id":"10.1074/jbc.m802286200"}],"title":"Trapping of the thioacylglyceraldehyde-3-phosphate dehydrogenase intermediate from Bacillus stearothermophilus. Direct evidence for a flip-flop mechanism.","publicationDate":"2008","journal":"J. Biol. Chem.","firstPage":"21693","lastPage":"21702","volume":"283"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD AND GLYCERALDEHYDE-3-PHOSPHATE","FUNCTION","ACTIVE SITE","REACTION MECHANISM","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M24493","properties":[{"key":"ProteinId","value":"AAA22461.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JS0164","properties":[{"key":"EntryName","value":"DEBSGF"}]},{"database":"RefSeq","id":"WP_033015082.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000002.1"}]},{"database":"PDB","id":"1DBV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"1GD1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"1NPT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.18 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"1NQ5","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.11 A"},{"key":"Chains","value":"A/C/O/Q=2-335"}]},{"database":"PDB","id":"1NQA","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"1NQO","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.01 A"},{"key":"Chains","value":"A/C/O/Q=2-335"}]},{"database":"PDB","id":"2DBV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"2GD1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"3CMC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.77 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"3DBV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.45 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"PDB","id":"4DBV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"O/P/Q/R=2-335"}]},{"database":"AlphaFoldDB","id":"P00362","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P00362","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB02263","properties":[{"key":"GenericName","value":"D-glyceraldehyde 3-phosphate"}]},{"database":"GeneID","id":"89613291","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803304at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.2.1.12","properties":[{"key":"OrganismId","value":"623"}]},{"database":"SABIO-RK","id":"P00362","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00184"}]},{"database":"EvolutionaryTrace","id":"P00362","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004365","properties":[{"key":"GoTerm","value":"F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"12569100"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"18480053"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006006","properties":[{"key":"GoTerm","value":"P:glucose metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd18126","properties":[{"key":"EntryName","value":"GAPDH_I_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05214","properties":[{"key":"EntryName","value":"GAPDH_I_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.360.10:FF:000002","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000001","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020831","properties":[{"key":"EntryName","value":"GlycerAld/Erythrose_P_DH"}]},{"database":"InterPro","id":"IPR020830","properties":[{"key":"EntryName","value":"GlycerAld_3-P_DH_AS"}]},{"database":"InterPro","id":"IPR020829","properties":[{"key":"EntryName","value":"GlycerAld_3-P_DH_cat"}]},{"database":"InterPro","id":"IPR020828","properties":[{"key":"EntryName","value":"GlycerAld_3-P_DH_NAD(P)-bd"}]},{"database":"InterPro","id":"IPR006424","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-P_DH_1"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01534","properties":[{"key":"EntryName","value":"GAPDH-I"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43148","properties":[{"key":"EntryName","value":"GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02800","properties":[{"key":"EntryName","value":"Gp_dh_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00044","properties":[{"key":"EntryName","value":"Gp_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000149","properties":[{"key":"EntryName","value":"GAP_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00078","properties":[{"key":"EntryName","value":"G3PDHDRGNASE"}]},{"database":"SMART","id":"SM00846","properties":[{"key":"EntryName","value":"Gp_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00071","properties":[{"key":"EntryName","value":"GAPDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL","length":335,"molWeight":36075,"crc64":"DBAAA2DD24497E18","md5":"8D272723B791611B29340FCA2D4E0A3E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":11,"Site":1,"Mutagenesis":5,"Beta strand":19,"Helix":14,"Turn":8},"uniParcId":"UPI000016E86A"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P14412","uniProtkbId":"KATG_GEOSE","entryAudit":{"firstPublicDate":"1990-01-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-02-01","entryVersion":119,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"katG"},"synonyms":[{"value":"cat"},{"value":"perA"}]}],"comments":[{"texts":[{"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Also displays NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activities"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":5670.0,"unit":"umol/min/mg","enzyme":"enzyme for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]},{"velocity":3410.0,"unit":"umol/min/mg","enzyme":"enzyme for H(2)O(2) for the catalase reaction (at pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]},{"velocity":8.0,"unit":"umol/min/mg","enzyme":"enzyme for ABTS for the peroxidase reaction","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]}],"michaelisConstants":[{"constant":90.0,"unit":"mM","substrate":"H(2)O(2) for the catalase reaction (at pH 5.5-6.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]},{"constant":3.7,"unit":"mM","substrate":"H(2)O(2) for the catalase reaction (at pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]},{"constant":210.0,"unit":"mM","substrate":"H(2)O(2) for the peroxidase reaction","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]},{"constant":31.0,"unit":"mM","substrate":"ABTS for the peroxidase reaction","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178143"}],"value":"Optimum pH is 4.0 for the peroxidase reaction."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":735,"modifier":"EXACT"}},"description":"Catalase-peroxidase","featureId":"PRO_0000055567"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-100)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0575","category":"Molecular function","name":"Peroxidase"}],"references":[{"referenceNumber":1,"citation":{"id":"2670897","citationType":"journal article","authors":["Loprasert S.","Negoro S.","Okada H."],"citationCrossReferences":[{"database":"PubMed","id":"2670897"},{"database":"DOI","id":"10.1128/jb.171.9.4871-4875.1989"}],"title":"Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA).","publicationDate":"1989","journal":"J. Bacteriol.","firstPage":"4871","lastPage":"4875","volume":"171"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PARTIAL PROTEIN SEQUENCE"],"referenceComments":[{"value":"ATCC 8005 / IAM11001","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-2KMPT9D0KTN29","citationType":"submission","authors":["Trakulnaleamsai S.","Aihara S.","Miyai K.","Suga Y.","Yomo T.","Negoro S.","Urabe I."],"publicationDate":"FEB-1992","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["SEQUENCE REVISION"]},{"referenceNumber":3,"citation":{"id":"9920270","citationType":"journal article","authors":["Matsuura T.","Miyai K.","Trakulnaleaamsai S.","Yomo T.","Shima Y.","Miki S.","Yamamoto K.","Urabe I."],"citationCrossReferences":[{"database":"PubMed","id":"9920270"},{"database":"DOI","id":"10.1038/5232"}],"title":"Evolutionary molecular engineering by random elongation mutagenesis.","publicationDate":"1999","journal":"Nat. Biotechnol.","firstPage":"58","lastPage":"61","volume":"17"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":4,"citation":{"id":"18178143","citationType":"journal article","authors":["Singh R.","Wiseman B.","Deemagarn T.","Jha V.","Switala J.","Loewen P.C."],"citationCrossReferences":[{"database":"PubMed","id":"18178143"},{"database":"DOI","id":"10.1016/j.abb.2007.12.008"}],"title":"Comparative study of catalase-peroxidases (KatGs).","publicationDate":"2008","journal":"Arch. Biochem. Biophys.","firstPage":"207","lastPage":"214","volume":"471"},"referencePositions":["BIOPHYSICOCHEMICAL PROPERTIES"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M29876","properties":[{"key":"ProteinId","value":"AAA22655.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AB020234","properties":[{"key":"ProteinId","value":"BAA37114.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JS0520","properties":[{"key":"EntryName","value":"JS0520"}]},{"database":"AlphaFoldDB","id":"P14412","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P14412","properties":[{"key":"Description","value":"-"}]},{"database":"PeroxiBase","id":"2437","properties":[{"key":"EntryName","value":"GstCP01"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF6","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MENQNRQNAAQCPFHGSVTNQSSNRTTNKDWWPNQLNLSILHQHDRKTNPHDEEFNYAEEFQKLDYWALKEDLRKLMTESQDWWPADYGHYGPLFIRMAWHSAGTYRIGDGRGGASTGTQRFAPLNSWPDNANLDKARRLLWPIKKKYGNKISWADLFILAGNVAIESMGGKTIGFGGGRVDVWHPEEDVYWGSEKEWLASERYSGDRELENPLAAVQMGLIYVNPEGPDGKPDPKAAARDIRETFRRMGMNDEETVALIAGGHTFGKAHGAGPATHVGPEPEAAPIEAQGLGWISSYGKGKGSDTITSGIEGAWTPTPTQWDTSYFDMLFGYDWWLTKSPAGAWQWMAVDPDEKDLAPDAEDPSKKVPTMMMTTDLALRFDPEYEKIARRFHQNPEEFAEAFARAWFKLTHRDMGPKTRYLGPEVPKEDFIWQDPIPEVDYELTEAEIEEIKAKILNSGLTVSELVKTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNEPERLAKVLSVYEDIQRELPKKVSIADLIVLGGSAAVEKAARDAGFDVKVPFFPGRGDATQEQTDVESFAVLEPFADGFRNYQKQEYSVPPEELLVDKAQLLGLTAPEMTVLVGGLRVLGANYRDLPHGVFTDRIGVLTNDFFVNLLDMNYEWVPTDSGIYEIRDRKTGEVRWTATRVDLIFGSNSILRSYAEFYAQDDNQEKFVRDFINAWVKVMNADRFDLVKKARESVTA","length":735,"molWeight":82989,"crc64":"7131204A4BFABEF1","md5":"689705D1D648E419177D0D9AF4A98C36"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":2,"Active site":1,"Binding site":1,"Site":1,"Cross-link":2},"uniParcId":"UPI000012704B"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q02499","uniProtkbId":"KPYK_GEOSE","entryAudit":{"firstPublicDate":"1994-02-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1994-10-01","entryVersion":149,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3711058"}],"value":"Pyruvate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"PK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"2.7.1.40"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3711058"}],"value":"ATP:pyruvate 2-O-phosphotransferase"}}]},"genes":[{"geneName":{"value":"pyk"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"Catalyzes the phosphoryl transfer from phosphoenolpyruvate (PEP) to ADP to form pyruvate and ATP (PubMed:15749828, PubMed:3711058). Has a broad specificity for nucleoside diphosphates and can use ADP, GDP, IDP and UDP (PubMed:3711058)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pyruvate + ATP = phosphoenolpyruvate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18157"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.40","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:18159"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"Can also use manganese or cobalt."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"Can also use ammonium ions."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"Exhibits homotropic positive cooperativity for PEP (PubMed:3711058). Allosterically activated by ribose-5-phosphate, AMP and other nucleoside monophosphates but not by fructose-1,6-bisphosphate (PubMed:3711058)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.186,"unit":"mM","substrate":"PEP (in the presence of 0.1 mM ribose-5-phosphate)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"}],"value":"kcat is 3.204 sec(-1) (in the presence of 0.1 mM ribose-5-phosphate)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"Optimum pH is 7.2 at 30 degrees Celsius. Optimum pH is 6.8 at 60 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18511452"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18511452"}],"value":"Contains an extra C-terminal sequence (ECTS), which contains a highly conserved PEP binding motif"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3711058"}],"value":"The N-terminus is blocked"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the pyruvate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the PEP-utilizing enzyme family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"CAA40994.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":587,"modifier":"EXACT"}},"description":"Pyruvate kinase","featureId":"PRO_0000112055"},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14618"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14618"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14618"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30613"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00549"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15749828"}]},{"type":"Mutagenesis","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Slight decrease in activity; when associated with S-268.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"10000 to 100000-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["C","D","L","R"]}},{"type":"Mutagenesis","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Slight decrease in activity; when associated with S-9.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Reduced activity; when associated with Y-416.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1447787"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"Increased activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1447787"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["Y"]}},{"type":"Mutagenesis","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"Decreases affinity for allosteric activators.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18511452"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"Does not affect kinetic properties.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18511452"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["E","K","R"]}},{"type":"Beta strand","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Turn","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Turn","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Turn","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Turn","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":451,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":482,"modifier":"EXACT"},"end":{"value":486,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":511,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":529,"modifier":"EXACT"},"end":{"value":535,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":541,"modifier":"EXACT"},"end":{"value":549,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":553,"modifier":"EXACT"},"end":{"value":555,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Helix","location":{"start":{"value":560,"modifier":"EXACT"},"end":{"value":563,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":569,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Turn","location":{"start":{"value":574,"modifier":"EXACT"},"end":{"value":577,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]},{"type":"Beta strand","location":{"start":{"value":578,"modifier":"EXACT"},"end":{"value":582,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2E28"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0630","category":"Ligand","name":"Potassium"},{"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"8436141","citationType":"journal article","authors":["Sakai H.","Ohta T."],"citationCrossReferences":[{"database":"PubMed","id":"8436141"},{"database":"DOI","id":"10.1111/j.1432-1033.1993.tb17618.x"}],"title":"Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon.","publicationDate":"1993","journal":"Eur. J. Biochem.","firstPage":"851","lastPage":"859","volume":"211"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 328-346 AND 393-396"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"1447787","citationType":"journal article","authors":["Walker D.","Chia W.N.","Muirhead H."],"citationCrossReferences":[{"database":"PubMed","id":"1447787"},{"database":"DOI","id":"10.1016/0022-2836(92)90505-e"}],"title":"Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis.","publicationDate":"1992","journal":"J. Mol. Biol.","firstPage":"265","lastPage":"276","volume":"228"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 1-51","MUTAGENESIS OF ASP-308 AND TRP-416"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"3711058","citationType":"journal article","authors":["Sakai H.","Suzuki K.","Imahori K."],"citationCrossReferences":[{"database":"PubMed","id":"3711058"},{"database":"DOI","id":"10.1093/oxfordjournals.jbchem.a135579"}],"title":"Purification and properties of pyruvate kinase from Bacillus stearothermophilus.","publicationDate":"1986","journal":"J. Biochem.","firstPage":"1157","lastPage":"1167","volume":"99"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"]},{"referenceNumber":4,"citation":{"id":"15749828","citationType":"journal article","authors":["Sakai H."],"citationCrossReferences":[{"database":"PubMed","id":"15749828"},{"database":"DOI","id":"10.1093/jb/mvi027"}],"title":"Mutagenesis of the active site lysine 221 of the pyruvate kinase from Bacillus stearothermophilus.","publicationDate":"2005","journal":"J. Biochem.","firstPage":"141","lastPage":"145","volume":"137"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","MUTAGENESIS OF CYS-9; LYS-221 AND CYS-268"]},{"referenceNumber":5,"citation":{"id":"16511150","citationType":"journal article","authors":["Suzuki K.","Ito S.","Shimizu-Ibuka A.","Sakai H."],"citationCrossReferences":[{"database":"PubMed","id":"16511150"},{"database":"DOI","id":"10.1107/s1744309105021093"}],"title":"Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus.","publicationDate":"2005","journal":"Acta Crystallogr. F","firstPage":"759","lastPage":"761","volume":"61"},"referencePositions":["CRYSTALLIZATION"]},{"referenceNumber":6,"citation":{"id":"18511452","citationType":"journal article","authors":["Suzuki K.","Ito S.","Shimizu-Ibuka A.","Sakai H."],"citationCrossReferences":[{"database":"PubMed","id":"18511452"},{"database":"DOI","id":"10.1093/jb/mvn069"}],"title":"Crystal structure of pyruvate kinase from Geobacillus stearothermophilus.","publicationDate":"2008","journal":"J. Biochem.","firstPage":"305","lastPage":"312","volume":"144"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANT SER-9/SER-268","SUBUNIT","DOMAIN","MUTAGENESIS OF HIS-425 AND VAL-435"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"2E28"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D13095","properties":[{"key":"ProteinId","value":"BAA02406.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X57859","properties":[{"key":"ProteinId","value":"CAA40994.1"},{"key":"Status","value":"ALT_FRAME"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S27330","properties":[{"key":"EntryName","value":"S27330"}]},{"database":"PIR","id":"S29783","properties":[{"key":"EntryName","value":"S29783"}]},{"database":"RefSeq","id":"WP_033014443.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000002.1"}]},{"database":"PDB","id":"2E28","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A=1-587"}]},{"database":"AlphaFoldDB","id":"Q02499","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q02499","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"89612056","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9812123at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.7.1.40","properties":[{"key":"OrganismId","value":"623"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00188"}]},{"database":"EvolutionaryTrace","id":"Q02499","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030955","properties":[{"key":"GoTerm","value":"F:potassium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004743","properties":[{"key":"GoTerm","value":"F:pyruvate kinase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15749828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3711058"}]},{"database":"GO","id":"GO:0006950","properties":[{"key":"GoTerm","value":"P:response to stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00288","properties":[{"key":"EntryName","value":"Pyruvate_Kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.33.10:FF:000001","properties":[{"key":"EntryName","value":"Pyruvate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.60:FF:000025","properties":[{"key":"EntryName","value":"Pyruvate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1380.20:FF:000007","properties":[{"key":"EntryName","value":"Pyruvate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.10:FF:000004","properties":[{"key":"EntryName","value":"Pyruvate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.60","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate-binding domains"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.10","properties":[{"key":"EntryName","value":"Phosphohistidine domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.33.10","properties":[{"key":"EntryName","value":"PK beta-barrel domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1380.20","properties":[{"key":"EntryName","value":"Pyruvate kinase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008279","properties":[{"key":"EntryName","value":"PEP-util_enz_mobile_dom"}]},{"database":"InterPro","id":"IPR036637","properties":[{"key":"EntryName","value":"Phosphohistidine_dom_sf"}]},{"database":"InterPro","id":"IPR001697","properties":[{"key":"EntryName","value":"Pyr_Knase"}]},{"database":"InterPro","id":"IPR015813","properties":[{"key":"EntryName","value":"Pyrv/PenolPyrv_kinase-like_dom"}]},{"database":"InterPro","id":"IPR040442","properties":[{"key":"EntryName","value":"Pyrv_kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR011037","properties":[{"key":"EntryName","value":"Pyrv_Knase-like_insert_dom_sf"}]},{"database":"InterPro","id":"IPR018209","properties":[{"key":"EntryName","value":"Pyrv_Knase_AS"}]},{"database":"InterPro","id":"IPR015793","properties":[{"key":"EntryName","value":"Pyrv_Knase_brl"}]},{"database":"InterPro","id":"IPR015795","properties":[{"key":"EntryName","value":"Pyrv_Knase_C"}]},{"database":"InterPro","id":"IPR036918","properties":[{"key":"EntryName","value":"Pyrv_Knase_C_sf"}]},{"database":"InterPro","id":"IPR015806","properties":[{"key":"EntryName","value":"Pyrv_Knase_insert_dom_sf"}]},{"database":"NCBIfam","id":"NF004491","properties":[{"key":"EntryName","value":"PRK05826.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004978","properties":[{"key":"EntryName","value":"PRK06354.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01064","properties":[{"key":"EntryName","value":"pyruv_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11817","properties":[{"key":"EntryName","value":"PYRUVATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00391","properties":[{"key":"EntryName","value":"PEP-utilizers"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00224","properties":[{"key":"EntryName","value":"PK"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02887","properties":[{"key":"EntryName","value":"PK_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01050","properties":[{"key":"EntryName","value":"PYRUVTKNASE"}]},{"database":"SUPFAM","id":"SSF51621","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate/pyruvate domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52009","properties":[{"key":"EntryName","value":"Phosphohistidine domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50800","properties":[{"key":"EntryName","value":"PK beta-barrel domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52935","properties":[{"key":"EntryName","value":"PK C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00110","properties":[{"key":"EntryName","value":"PYRUVATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRKTKIVCTIGPASESVDKLVQLMEAGMNVARLNFSHGDHEEHGRRIANIREAAKRTGRTVAILLDTKGPEIRTHNMENGAIELKEGSKLVISMSEVLGTPEKISVTYPSLIDDVSVGAKILLDDGLISLEVNAVDKQAGEIVTTVLNGGVLKNKKGVNVPGVKVNLPGITEKDRADILFGIRQGIDFIAASFVRRASDVLEIRELLEAHDALHIQIIAKIENEEGVANIDEILEAADGLMVARGDLGVEIPAEEVPLIQKLLIKKCNMLGKPVITATQMLDSMQRNPRPTRAEASDVANAIFDGTDAVMLSGETAAGQYPVEAVKTMHQIALRTEQALEHRDILSQRTKESQTTITDAIGQSVAHTALNLDVAAIVTPTVSGKTPQMVAKYRPKAPIIAVTSNEAVSRRLALVWGVYTKEAPHVNTTDEMLDVAVDAAVRSGLVKHGDLVVITAGVPVGETGSTNLMKVHVISDLLAKGQGIGRKSAFGKAVVAKTAEEARQKMVDGGILVTVSTDADMMPAIEKAAAIITEEGGLTSHAAVVGLSLGIPVIVGVENATTLFKDGQEITVDGGFGAVYRGHASVL","length":587,"molWeight":62318,"crc64":"0794BA1A07BE0D5A","md5":"CA74CFE028D5AE64EB0EA75024650B6B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"DOMAIN":1,"PTM":1,"SIMILARITY":2,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Binding site":14,"Site":1,"Mutagenesis":7,"Beta strand":28,"Turn":5,"Helix":24},"uniParcId":"UPI000012E00B"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q7SIB1","uniProtkbId":"CCA_GEOSE","entryAudit":{"firstPublicDate":"2005-08-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2003-12-15","entryVersion":84,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"CCA-adding enzyme"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P06961"},{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"2.7.7.72"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"CCA tRNA nucleotidyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"tRNA CCA-pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"tRNA adenylyl-/cytidylyl- transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"tRNA nucleotidyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"tRNA-NT"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}],"value":"cca"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O28126"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P06961"}],"value":"Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded (By similarity). The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA. This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14433"},{"database":"Rhea","id":"RHEA-COMP:10465"},{"database":"Rhea","id":"RHEA-COMP:10468"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:74896"},{"database":"ChEBI","id":"CHEBI:83071"}],"ecNumber":"2.7.7.72","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P06961"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a tRNA with a 3' CCA end + 2 CTP + ATP = a tRNA with a 3' CCACCA end + 3 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:76235"},{"database":"Rhea","id":"RHEA-COMP:10468"},{"database":"Rhea","id":"RHEA-COMP:18655"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:83071"},{"database":"ChEBI","id":"CHEBI:195187"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:76236"},"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O28126"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"}],"value":"The crystal structure reveals a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head domain contains the nucleotidyltransferase activity. The neck domain provides a specific template for the incoming ATP or CTP, whereas the body and tail domains may be involved in tRNA binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"}],"value":"A single active site specifically recognizes both ATP and CTP and is responsible for their addition"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01263"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 3 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"CCA-adding enzyme","featureId":"PRO_0000139033"},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O28126"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O28126"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12526808"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"May assist in discriminating ATP from CTP"},{"type":"Site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Involved in nucleotide selection","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Helix","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIV"}]},{"type":"Beta strand","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIV"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIV"}]},{"type":"Helix","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Beta strand","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Turn","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]},{"type":"Helix","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MIW"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0692","category":"Biological process","name":"RNA repair"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"12526808","citationType":"journal article","authors":["Li F.","Xiong Y.","Wang J.","Cho H.D.","Tomita K.","Weiner A.M.","Steitz T.A."],"citationCrossReferences":[{"database":"PubMed","id":"12526808"},{"database":"DOI","id":"10.1016/s0092-8674(02)01115-7"}],"title":"Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.","publicationDate":"2002","journal":"Cell","firstPage":"815","lastPage":"824","volume":"111"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","X-RAY CRYSTALLOGRAPHY OF NATIVE PROTEIN AND COMPLEXES WITH ATP AND CTP","SUBUNIT"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIV"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIW"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MIY"}]}],"uniProtKBCrossReferences":[{"database":"PDB","id":"1MIV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.50 A"},{"key":"Chains","value":"A/B=1-404"}]},{"database":"PDB","id":"1MIW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A/B=1-404"}]},{"database":"PDB","id":"1MIY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.52 A"},{"key":"Chains","value":"A/B=1-404"}]},{"database":"AlphaFoldDB","id":"Q7SIB1","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q7SIB1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q7SIB1","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB02431","properties":[{"key":"GenericName","value":"Cytidine-5'-Triphosphate"}]},{"database":"BRENDA","id":"2.7.7.72","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"Q7SIB1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004810","properties":[{"key":"GoTerm","value":"F:CCA tRNA nucleotidyltransferase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0160016","properties":[{"key":"GoTerm","value":"F:CCACCA tRNA nucleotidyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0001680","properties":[{"key":"GoTerm","value":"P:tRNA 3'-terminal CCA addition"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05398","properties":[{"key":"EntryName","value":"NT_ClassII-CCAase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.110.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.246.80","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.560","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.460.10","properties":[{"key":"EntryName","value":"Beta Polymerase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01263","properties":[{"key":"EntryName","value":"CCA_bact_type3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050264","properties":[{"key":"EntryName","value":"Bact_CCA-adding_enz_type3_sf"}]},{"database":"InterPro","id":"IPR032810","properties":[{"key":"EntryName","value":"CCA-adding_enz_C"}]},{"database":"InterPro","id":"IPR023068","properties":[{"key":"EntryName","value":"CCA-adding_enz_firmicutes"}]},{"database":"InterPro","id":"IPR043519","properties":[{"key":"EntryName","value":"NT_sf"}]},{"database":"InterPro","id":"IPR002646","properties":[{"key":"EntryName","value":"PolA_pol_head_dom"}]},{"database":"InterPro","id":"IPR032828","properties":[{"key":"EntryName","value":"PolyA_RNA-bd"}]},{"database":"NCBIfam","id":"NF009814","properties":[{"key":"EntryName","value":"PRK13299.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46173","properties":[{"key":"EntryName","value":"CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46173:SF1","properties":[{"key":"EntryName","value":"CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01743","properties":[{"key":"EntryName","value":"PolyA_pol"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12627","properties":[{"key":"EntryName","value":"PolyA_pol_RNAbd"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13735","properties":[{"key":"EntryName","value":"tRNA_NucTran2_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81301","properties":[{"key":"EntryName","value":"Nucleotidyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81891","properties":[{"key":"EntryName","value":"Poly A polymerase C-terminal region-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKPPFQEALGIIQQLKQHGYDAYFVGGAVRDLLLGRPIGDVDIATSALPEDVMAIFPKTIDVGSKHGTVVVVHKGKAYEVTTFKTDGDYEDYRRPESVTFVRSLEEDLKRRDFTMNAIAMDEYGTIIDPFGGREAIRRRIIRTVGEAEKRFREDALRMMRAVRFVSELGFALAPDTEQAIVQNAPLLAHISVERMTMEMEKLLGGPFAARALPLLAETGLNAYLPGLAGKEKQLRLAAAYRWPWLAAREERWALLCHALGVQESRPFLRAWKLPNKVVDEAGAILTALADIPRPEAWTNEQLFSAGLERALSVETVRAAFTGAPPGPWHEKLRRRFASLPIKTKGELAVNGKDVIEWVGKPAGPWVKEALDAIWRAVVNGEVENEKERIYAWLMERNRTREKNC","length":404,"molWeight":45369,"crc64":"DC0C8E4C47133940","md5":"4196736B421708FC71268AD977A45C04"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":16,"Site":2,"Helix":27,"Beta strand":11,"Turn":1},"uniParcId":"UPI0000112631"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9XBQ3","uniProtkbId":"IABF_GEOSE","entryAudit":{"firstPublicDate":"2002-07-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":96,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Intracellular exo-alpha-(1->5)-L-arabinofuranosidase"},"shortNames":[{"value":"ABF"}],"ecNumbers":[{"value":"3.2.1.55"}]},"alternativeNames":[{"fullName":{"value":"Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase"},"shortNames":[{"value":"Arabinosidase"}]}]},"genes":[{"geneName":{"value":"abfA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}],"value":"Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on aryl-alpha-L-arabinofuranosides, and is much less effective on aryl-beta-D-xylopyranosides"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.","ecNumber":"3.2.1.55","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}],"value":"Strongly inhibited by Hg(2+)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":749.0,"unit":"umol/min/mg","enzyme":"enzyme (at 60 degrees Celsius and at pH 6)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]}],"michaelisConstants":[{"constant":0.35,"unit":"mM","substrate":"2,5-dinitro-arabinofuranosyl","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"constant":0.42,"unit":"mM","substrate":"p-nitrophenyl alpha-L-arabinofuranoside (pNP-Araf) (at 60 degrees Celsius and at pH 6)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"constant":0.53,"unit":"mM","substrate":"3,4-dinitro-arabinofuranosyl","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"constant":0.65,"unit":"mM","substrate":"4-nitro-arabinofuranosyl","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"constant":4.4,"unit":"mM","substrate":"3,4-dinitro-xylopyranosyl","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"constant":8.0,"unit":"mM","substrate":"2,5-dinitro-xylopyranosyl","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"constant":15.3,"unit":"mM","substrate":"2-nitro-xylopyranosyl","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"}],"value":"Apparently, AbfA can accommodate xylopyranose in the active site, but without the necessary distortion required for the efficient catalysis of six-membered rings. This explains in part its lower specificity towards the xylopyranosidic substrates."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}],"value":"Optimum pH is 5.5-6.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}],"value":"Optimum temperature is 70 degrees Celsius."}]}},{"texts":[{"value":"Glycan metabolism; L-arabinan degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12777810"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7887599"}],"value":"Homohexamer; trimer of dimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P94531"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7887599"}],"value":"Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene (Probable)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 51 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7887599"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":502,"modifier":"EXACT"}},"description":"Intracellular exo-alpha-(1->5)-L-arabinofuranosidase","featureId":"PRO_0000057700"},{"type":"Active site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14517232"}]},{"type":"Active site","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14517232"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"Important for substrate recognition","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14517232"}]},{"type":"Site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"Important for substrate recognition","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14517232"}]},{"type":"Mutagenesis","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Strongly reduced catalytic activity. Increases affinity for substrates. The mutant has an effect on the glycosylation step. The removal of the acid-base catalyst seems to have affected the ionization state of the nucleophile, elevating its pKa, reducing its acidity, and shifting the optimal pH to higher values.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Abolishes catalytic activity, but the binding affinity shows only a small change.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12221104"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Turn","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Turn","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Turn","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Turn","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Turn","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Helix","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Turn","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":430,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PZ3"}]},{"type":"Beta strand","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":447,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":473,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PZ3"}]},{"type":"Beta strand","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":484,"modifier":"EXACT"},"end":{"value":489,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]},{"type":"Beta strand","location":{"start":{"value":491,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1QW9"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8SE5C6HIMCKTL","citationType":"submission","authors":["Gilead-Gropper S.","Gat O.","Alchanati I.","Yaron S.","Bren A.","Shoham Y."],"publicationDate":"NOV-2001","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"T-6 / NCIMB 40222","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"7887599","citationType":"journal article","authors":["Gilead S.","Shoham Y."],"citationCrossReferences":[{"database":"PubMed","id":"7887599"},{"database":"DOI","id":"10.1128/aem.61.1.170-174.1995"}],"title":"Purification and characterization of alpha-L-arabinofuranosidase from Bacillus stearothermophilus T-6.","publicationDate":"1995","journal":"Appl. Environ. Microbiol.","firstPage":"170","lastPage":"174","volume":"61"},"referencePositions":["PROTEIN SEQUENCE OF 2-51","FUNCTION","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","INDUCTION","SUBUNIT"],"referenceComments":[{"value":"T-6 / NCIMB 40222","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"11943144","citationType":"journal article","authors":["Shallom D.","Belakhov V.","Solomon D.","Gilead-Gropper S.","Baasov T.","Shoham G.","Shoham Y."],"citationCrossReferences":[{"database":"PubMed","id":"11943144"},{"database":"DOI","id":"10.1016/s0014-5793(02)02343-8"}],"title":"The identification of the acid-base catalyst of alpha-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase.","publicationDate":"2002","journal":"FEBS Lett.","firstPage":"163","lastPage":"167","volume":"514"},"referencePositions":["FUNCTION","MUTAGENESIS OF GLU-175","ACTIVE SITE","BIOPHYSICOCHEMICAL PROPERTIES","REACTION MECHANISM"]},{"referenceNumber":4,"citation":{"id":"12221104","citationType":"journal article","authors":["Shallom D.","Belakhov V.","Solomon D.","Shoham G.","Baasov T.","Shoham Y."],"citationCrossReferences":[{"database":"PubMed","id":"12221104"},{"database":"DOI","id":"10.1074/jbc.m208285200"}],"title":"Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase.","publicationDate":"2002","journal":"J. Biol. Chem.","firstPage":"43667","lastPage":"43673","volume":"277"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF GLU-175 AND GLU-294","ACTIVE SITE","BIOPHYSICOCHEMICAL PROPERTIES","REACTION MECHANISM"]},{"referenceNumber":5,"citation":{"id":"12777810","citationType":"journal article","authors":["Hovel K.","Shallom D.","Niefind K.","Baasov T.","Shoham G.","Shoham Y.","Schomburg D."],"citationCrossReferences":[{"database":"PubMed","id":"12777810"},{"database":"DOI","id":"10.1107/s0907444903004037"}],"title":"Crystallization and preliminary X-ray analysis of a family 51 glycoside hydrolase, the alpha-l-arabinofuranosidase from Geobacillus stearothermophilus T-6.","publicationDate":"2003","journal":"Acta Crystallogr. D","firstPage":"913","lastPage":"915","volume":"59"},"referencePositions":["SUBUNIT"]},{"referenceNumber":6,"citation":{"id":"14517232","citationType":"journal article","authors":["Hovel K.","Shallom D.","Niefind K.","Belakhov V.","Shoham G.","Baasov T.","Shoham Y.","Schomburg D."],"citationCrossReferences":[{"database":"PubMed","id":"14517232"},{"database":"DOI","id":"10.1093/emboj/cdg494"}],"title":"Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase.","publicationDate":"2003","journal":"EMBO J.","firstPage":"4922","lastPage":"4932","volume":"22"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANT ALA-175 IN COMPLEXES WITH FURANOSIDIC SUBSTRATES","FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF GLU-175","REACTION MECHANISM","ACTIVE SITE","BIOPHYSICOCHEMICAL PROPERTIES","SUBSTRATE SPECIFICITY","SUBUNIT"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1PZ3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1QW9"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF159625","properties":[{"key":"ProteinId","value":"AAD45520.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"1PZ2","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=1-502"}]},{"database":"PDB","id":"1PZ3","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A/B=1-502"}]},{"database":"PDB","id":"1QW8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=1-502"}]},{"database":"PDB","id":"1QW9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.20 A"},{"key":"Chains","value":"A/B=1-502"}]},{"database":"PDB","id":"6SXU","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"AAA/BBB=1-502"}]},{"database":"PDB","id":"6SXV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A/B=1-502"}]},{"database":"AlphaFoldDB","id":"Q9XBQ3","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q9XBQ3","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9XBQ3","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB03196","properties":[{"key":"GenericName","value":"4-Nitrophenyl-Ara"}]},{"database":"DrugBank","id":"DB03870","properties":[{"key":"GenericName","value":"Ara-Alpha(1,3)-Xyl"}]},{"database":"CAZy","id":"GH51","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 51"}]},{"database":"BRENDA","id":"3.2.1.55","properties":[{"key":"OrganismId","value":"623"}]},{"database":"UniPathway","id":"UPA00667","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q9XBQ3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0046556","properties":[{"key":"GoTerm","value":"F:alpha-L-arabinofuranosidase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517232"}]},{"database":"GO","id":"GO:0031222","properties":[{"key":"GoTerm","value":"P:arabinan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0046373","properties":[{"key":"GoTerm","value":"P:L-arabinose metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1180","properties":[{"key":"EntryName","value":"Golgi alpha-mannosidase II"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010720","properties":[{"key":"EntryName","value":"Alpha-L-AF_C"}]},{"database":"InterPro","id":"IPR055235","properties":[{"key":"EntryName","value":"ASD1_cat"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR013780","properties":[{"key":"EntryName","value":"Glyco_hydro_b"}]},{"database":"NCBIfam","id":"NF051901","properties":[{"key":"EntryName","value":"ArabsyFurArfAAgro"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43576:SF3","properties":[{"key":"EntryName","value":"ALPHA-L-ARABINOFURANOSIDASE C"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43576","properties":[{"key":"EntryName","value":"ALPHA-L-ARABINOFURANOSIDASE C-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06964","properties":[{"key":"EntryName","value":"Alpha-L-AF_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22848","properties":[{"key":"EntryName","value":"ASD1_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00813","properties":[{"key":"EntryName","value":"Alpha-L-AF_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51011","properties":[{"key":"EntryName","value":"Glycosyl hydrolase domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATKKATMIIEKDFKIAEIDKRIYGSFIEHLGRAVYGGIYEPGHPQADENGFRQDVIELVKELQVPIIRYPGGNFVSGYNWEDGVGPKEQRPRRLDLAWKSVETNEIGLNEFMDWAKMVGAEVNMAVNLGTRGIDAARNLVEYCNHPSGSYYSDLRIAHGYKEPHKIKTWCLGNEMDGPWQIGHKTAVEYGRIACEAAKVMKWVDPTIELVVCGSSNRNMPTFAEWEATVLDHTYDHVDYISLHQYYGNRDNDTANYLALSLEMDDFIRSVVAIADYVKAKKRSKKTIHLSFDEWNVWYHSNEADKLIEPWTVAPPLLEDIYNFEDALLVGCMLITLMKHADRVKIACLAQLVNVIAPIMTEKNGPAWKQTIYYPFMHASVYGRGVALHPVISSPKYDSKDFTDVPYLESIAVYNEEKEEVTIFAVNRDMEDALLLECDVRSFEDYRVIEHIVLEHDNVKQTNSAQSSPVVPHRNGDAQLSDRKVSATLPKLSWNVIRLGKR","length":502,"molWeight":57212,"crc64":"37C048AE29DBB230","md5":"6F37E5181BD4D159ADD317973D24ED98"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":2,"Binding site":6,"Site":2,"Mutagenesis":2,"Beta strand":29,"Helix":16,"Turn":6},"uniParcId":"UPI000016E3DF"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"C3W947","uniProtkbId":"CTSR_GEOSE","entryAudit":{"firstPublicDate":"2014-09-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-06-16","entryVersion":48,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Transcriptional regulator CtsR"}},"alternativeNames":[{"fullName":{"value":"Class three stress gene repressor"}}]},"genes":[{"geneName":{"value":"ctsr"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB, by acting as a repressor of these class III stress genes. After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}],"value":"Repressor activity is controlled via phosphorylation on arginine residues. Unphosphorylated CtsR binds with high affinity to its DNA consensus site and inhibits transcription of downstream genes, whereas the McsB-phosphorylated CtsR repressor is not able to bind to DNA, thus allowing heat-shock gene expression (PubMed:19498169)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"CtsR autoinduces its own synthesis by derepression of the clpC operon after heat shock"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}],"value":"Is composed of two distinct domains: an N-terminal DNA binding domain that adopts the winged HTH fold (residues 2-72) and a C-terminal dimerization domain (residues 79-153) that consists of four alpha helices organized in a four-helix bundle"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}],"value":"Phosphorylated on Arg-28, Arg-49 and Arg-62 by McsB"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the CtsR family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Transcriptional regulator CtsR","featureId":"PRO_0000430098"},{"type":"Region","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"Interaction with DNA"},{"type":"Region","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Interaction with DNA"},{"type":"Region","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Interaction with DNA"},{"type":"Region","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Interaction with DNA"},{"type":"Site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Interaction with DNA"},{"type":"Site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Important for DNA binding"},{"type":"Modified residue","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Phosphoarginine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}]},{"type":"Modified residue","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Phosphoarginine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}]},{"type":"Modified residue","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Phosphoarginine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}]},{"type":"Mutagenesis","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Loss of the capability to bind DNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"No alteration of the capability to bind DNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19498169"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["K"]}},{"type":"Helix","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Beta strand","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Beta strand","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Beta strand","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]},{"type":"Helix","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H0D"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0678","category":"Molecular function","name":"Repressor"},{"id":"KW-0346","category":"Biological process","name":"Stress response"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-FMOC2K2HL7RV1","citationType":"submission","authors":["Fuhrmann J."],"title":"Characterization of CtsR from Bacillus stearothermophilus.","publicationDate":"APR-2009","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"19498169","citationType":"journal article","authors":["Fuhrmann J.","Schmidt A.","Spiess S.","Lehner A.","Turgay K.","Mechtler K.","Charpentier E.","Clausen T."],"citationCrossReferences":[{"database":"PubMed","id":"19498169"},{"database":"DOI","id":"10.1126/science.1170088"}],"title":"McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR.","publicationDate":"2009","journal":"Science","firstPage":"1323","lastPage":"1327","volume":"324"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH DNA","REGULATION","SUBUNIT","DOMAIN","PHOSPHORYLATION AT ARG-28; ARG-49 AND ARG-62","MUTAGENESIS OF ARG-62"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FN376878","properties":[{"key":"ProteinId","value":"CAY26036.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_033017268.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000002.1"}]},{"database":"PDB","id":"3H0D","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B=2-153"}]},{"database":"AlphaFoldDB","id":"C3W947","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"C3W947","properties":[{"key":"Description","value":"-"}]},{"database":"iPTMnet","id":"C3W947","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"89612930","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1680813at2","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"C3W947","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006355","properties":[{"key":"GoTerm","value":"P:regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.30.56.130:FF:000001","properties":[{"key":"EntryName","value":"Transcriptional regulator CtsR"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1200.150","properties":[{"key":"EntryName","value":"Transcriptional regulator CtsR, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.56.130","properties":[{"key":"EntryName","value":"Transcriptional regulator CtsR, winged HTH domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008463","properties":[{"key":"EntryName","value":"CtsR"}]},{"database":"InterPro","id":"IPR041473","properties":[{"key":"EntryName","value":"CtsR_C"}]},{"database":"InterPro","id":"IPR041908","properties":[{"key":"EntryName","value":"CtsR_C_sf"}]},{"database":"InterPro","id":"IPR040465","properties":[{"key":"EntryName","value":"CtsR_N"}]},{"database":"InterPro","id":"IPR041902","properties":[{"key":"EntryName","value":"CtsR_N_sf"}]},{"database":"Pfam","id":"PF05848","properties":[{"key":"EntryName","value":"CtsR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17727","properties":[{"key":"EntryName","value":"CtsR_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF010607","properties":[{"key":"EntryName","value":"Txn_repr_CtsR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPNISDIIEQYLKQVLNMSDQDIVEIKRSEIANKFRCVPSQINYVINTRFTLERGYIVESKRGGGGYIRIMKVKTKSEAQLIDQLLELIDHRISQSSAEDVIKRLMEEKVISEREAKMMLSVMDRSVLYIDLPERDELRARMLKAMLTSLKYK","length":153,"molWeight":17872,"crc64":"4C37E27E00CEA061","md5":"AAEE2BA8E8D8C133FFF41C1A969AA7F6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"INDUCTION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":4,"Site":2,"Modified residue":3,"Mutagenesis":2,"Helix":9,"Beta strand":3},"uniParcId":"UPI00019D047C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00943","uniProtkbId":"TPIS_GEOSE","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1992-12-01","entryVersion":136,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8421318"}],"value":"Triosephosphate isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8421318"}],"value":"TIM"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8421318"}],"value":"TPI"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}],"value":"5.3.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8421318"}],"value":"Triose-phosphate isomerase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}],"value":"tpiA"},"synonyms":[{"value":"tpi"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8421318"}],"value":"Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18585"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"5.3.1.1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8421318"}],"value":"Optimum temperature is 60 degrees Celsius (PubMed:8421318). Thermostable (PubMed:10383424)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8580851"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Belongs to the triosephosphate isomerase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Triosephosphate isomerase","featureId":"PRO_0000090178"},{"type":"Active site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Electrophile","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8580851"}]},{"type":"Active site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10383424"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8580851"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8580851"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8580851"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8580851"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00147"}]},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Displays poor thermostability, with an inactivation temperature of 37 degrees Celsius; when associated with G-14.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"Displays poor thermostability, with an inactivation temperature of 37 degrees Celsius; when associated with N-13.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383424"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["G"]}},{"type":"Sequence conflict","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"I","alternativeSequences":["D"]}},{"type":"Sequence conflict","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{}},{"type":"Sequence conflict","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{}},{"type":"Sequence conflict","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["LQ"]}},{"type":"Sequence conflict","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["H"]}},{"type":"Sequence conflict","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Sequence conflict","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"QTN","alternativeSequences":["ETD"]}},{"type":"Sequence conflict","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{}},{"type":"Sequence conflict","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"EQ","alternativeSequences":["QE"]}},{"type":"Sequence conflict","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"QAVI","alternativeSequences":["IIL"]}},{"type":"Sequence conflict","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"I","alternativeSequences":["L"]}},{"type":"Sequence conflict","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Beta strand","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Turn","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Turn","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Turn","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Turn","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Beta strand","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]},{"type":"Helix","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2BTM"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"}],"references":[{"referenceNumber":1,"citation":{"id":"8421318","citationType":"journal article","authors":["Rentier-Delrue F.","Mande S.C.","Moyens S.","Terpstra P.","Mainfroid V.","Goraj K.","Lion M.","Hol W.G.J.","Martial J.A."],"citationCrossReferences":[{"database":"PubMed","id":"8421318"},{"database":"DOI","id":"10.1006/jmbi.1993.1010"}],"title":"Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences.","publicationDate":"1993","journal":"J. Mol. Biol.","firstPage":"85","lastPage":"93","volume":"229"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","BIOPHYSICOCHEMICAL PROPERTIES"]},{"referenceNumber":2,"citation":{"id":"8244026","citationType":"journal article","authors":["Rentier-Delrue F.","Moyens S.","Lion M.","Martial J.A."],"citationCrossReferences":[{"database":"PubMed","id":"8244026"},{"database":"DOI","id":"10.1016/0378-1119(93)90188-9"}],"title":"Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus.","publicationDate":"1993","journal":"Gene","firstPage":"137","lastPage":"138","volume":"134"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":3,"citation":{"id":"6105959","citationType":"journal article","authors":["Artavanis-Tsakonas S.","Harris J.I."],"citationCrossReferences":[{"database":"PubMed","id":"6105959"},{"database":"DOI","id":"10.1111/j.1432-1033.1980.tb04755.x"}],"title":"Primary structure of triosephosphate isomerase from Bacillus stearothermophilus.","publicationDate":"1980","journal":"Eur. J. Biochem.","firstPage":"599","lastPage":"611","volume":"108"},"referencePositions":["PRELIMINARY PROTEIN SEQUENCE"]},{"referenceNumber":4,"citation":{"id":"8580851","citationType":"journal article","authors":["Delboni L.F.","Mande S.C.","Rentier-Delrue F.","Mainfroid V.","Turley S.","Vellieux F.M.D.","Martial J.A.","Hol W.G.J."],"citationCrossReferences":[{"database":"PubMed","id":"8580851"},{"database":"DOI","id":"10.1002/pro.5560041217"}],"title":"Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.","publicationDate":"1995","journal":"Protein Sci.","firstPage":"2594","lastPage":"2604","volume":"4"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE ANALOG","SUBUNIT"]},{"referenceNumber":5,"citation":{"id":"10383424","citationType":"journal article","authors":["Alvarez M.","Wouters J.","Maes D.","Mainfroid V.","Rentier-Delrue F.","Wyns L.","Depiereux E.","Martial J.A."],"citationCrossReferences":[{"database":"PubMed","id":"10383424"},{"database":"DOI","id":"10.1074/jbc.274.27.19181"}],"title":"Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.","publicationDate":"1999","journal":"J. Biol. Chem.","firstPage":"19181","lastPage":"19187","volume":"274"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANT ASN-13 AND GLY-14 IN COMPLEX WITH SUBSTRATE ANALOG","MUTAGENESIS OF HIS-13 AND LYS-14","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66129","properties":[{"key":"ProteinId","value":"CAA46920.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JT0768","properties":[{"key":"EntryName","value":"ISBSTF"}]},{"database":"PDB","id":"1BTM","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A/B=2-253"}]},{"database":"PDB","id":"2BTM","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B=2-253"}]},{"database":"AlphaFoldDB","id":"P00943","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P00943","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB02726","properties":[{"key":"GenericName","value":"2-Phosphoglycolic Acid"}]},{"database":"BRENDA","id":"5.3.1.1","properties":[{"key":"OrganismId","value":"623"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00189"}]},{"database":"UniPathway","id":"UPA00138","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"P00943","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004807","properties":[{"key":"GoTerm","value":"F:triose-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046166","properties":[{"key":"GoTerm","value":"P:glyceraldehyde-3-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019563","properties":[{"key":"GoTerm","value":"P:glycerol catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00311","properties":[{"key":"EntryName","value":"TIM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000016","properties":[{"key":"EntryName","value":"Triosephosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00147_B","properties":[{"key":"EntryName","value":"TIM_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR035990","properties":[{"key":"EntryName","value":"TIM_sf"}]},{"database":"InterPro","id":"IPR022896","properties":[{"key":"EntryName","value":"TrioseP_Isoase_bac/euk"}]},{"database":"InterPro","id":"IPR000652","properties":[{"key":"EntryName","value":"Triosephosphate_isomerase"}]},{"database":"InterPro","id":"IPR020861","properties":[{"key":"EntryName","value":"Triosephosphate_isomerase_AS"}]},{"database":"NCBIfam","id":"TIGR00419","properties":[{"key":"EntryName","value":"tim"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21139","properties":[{"key":"EntryName","value":"TRIOSEPHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21139:SF42","properties":[{"key":"EntryName","value":"TRIOSEPHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00121","properties":[{"key":"EntryName","value":"TIM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51351","properties":[{"key":"EntryName","value":"Triosephosphate isomerase (TIM)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00171","properties":[{"key":"EntryName","value":"TIM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51440","properties":[{"key":"EntryName","value":"TIM_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRKPIIAGNWKMHKTLAEAVQFVEDVKGHVPPADEVISVVCAPFLFLDRLVQAADGTDLKIGAQTMHFADQGAYTGEVSPVMLKDLGVTYVILGHSERRQMFAETDETVNKKVLAAFTRGLIPIICCGESLEEREAGQTNAVVASQVEKALAGLTPEQVKQAVIAYEPIWAIGTGKSSTPEDANSVCGHIRSVVSRLFGPEAAEAIRIQYGGSVKPDNIRDFLAQQQIDGPLVGGASLEPASFLQLVEAGRHE","length":253,"molWeight":27206,"crc64":"6532B5235362946C","md5":"429E605813BB5B26501593840902C9E9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":4,"Modified residue":1,"Mutagenesis":2,"Sequence conflict":13,"Beta strand":9,"Helix":15,"Turn":4},"uniParcId":"UPI00001371DE"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P31797","uniProtkbId":"CDGT_GEOSE","entryAudit":{"firstPublicDate":"1993-07-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1993-07-01","entryVersion":144,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cyclomaltodextrin glucanotransferase"},"ecNumbers":[{"value":"2.4.1.19"}]},"alternativeNames":[{"fullName":{"value":"Cyclodextrin-glycosyltransferase"},"shortNames":[{"value":"CGTase"}]}],"flag":"Precursor"},"genes":[{"geneName":{"value":"cgt"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.","ecNumber":"2.4.1.19"}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"value":"Binds 2 calcium ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.3"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"value":"May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 13 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.2"}]},{"type":"Chain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":711,"modifier":"EXACT"}},"description":"Cyclomaltodextrin glucanotransferase","featureId":"PRO_0000001442"},{"type":"Domain","location":{"start":{"value":526,"modifier":"EXACT"},"end":{"value":604,"modifier":"EXACT"}},"description":"IPT/TIG"},{"type":"Domain","location":{"start":{"value":605,"modifier":"EXACT"},"end":{"value":711,"modifier":"EXACT"}},"description":"CBM20","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00594"}]},{"type":"Region","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"A1"},{"type":"Region","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"B"},{"type":"Region","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"A2"},{"type":"Region","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":522,"modifier":"EXACT"}},"description":"C"},{"type":"Region","location":{"start":{"value":523,"modifier":"EXACT"},"end":{"value":606,"modifier":"EXACT"}},"description":"D"},{"type":"Region","location":{"start":{"value":607,"modifier":"EXACT"},"end":{"value":711,"modifier":"EXACT"}},"description":"E"},{"type":"Active site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Nucleophile"},{"type":"Active site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Proton donor"},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":398,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":402,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Disulfide bond","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":""},{"type":"Sequence conflict","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"in Ref. 2; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["R"]}},{"type":"Beta strand","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Turn","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Turn","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Turn","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Turn","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Turn","location":{"start":{"value":486,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":500,"modifier":"EXACT"},"end":{"value":502,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":527,"modifier":"EXACT"},"end":{"value":532,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":536,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":541,"modifier":"EXACT"},"end":{"value":547,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":555,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":570,"modifier":"EXACT"},"end":{"value":576,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":582,"modifier":"EXACT"},"end":{"value":590,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":600,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":610,"modifier":"EXACT"},"end":{"value":619,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":627,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":635,"modifier":"EXACT"},"end":{"value":637,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Helix","location":{"start":{"value":642,"modifier":"EXACT"},"end":{"value":644,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":652,"modifier":"EXACT"},"end":{"value":655,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":660,"modifier":"EXACT"},"end":{"value":669,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":687,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":693,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":699,"modifier":"EXACT"},"end":{"value":701,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]},{"type":"Beta strand","location":{"start":{"value":703,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1CYG"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0106","category":"Ligand","name":"Calcium"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"1476442","citationType":"journal article","authors":["Fujiwara S.","Kakihara H.","Woo K.B.","Lejeune A.","Kanemoto M.","Sakaguchi K.","Imanaka T."],"citationCrossReferences":[{"database":"PubMed","id":"1476442"},{"database":"DOI","id":"10.1128/aem.58.12.4016-4025.1992"}],"title":"Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme.","publicationDate":"1992","journal":"Appl. Environ. Microbiol.","firstPage":"4016","lastPage":"4025","volume":"58"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"NO. 2","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-5A8RV2AMBE8ND","citationType":"patent","authors":["Sugimoto T.","Kubota M.","Sakai S."],"title":"Polypeptide possessing cyclomaltodextrin glucanotransferase activity.","publicationDate":"23-JUL-1986","patentNumber":"GB2169902"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 32-41"]},{"referenceNumber":3,"citation":{"id":"CI-B90VIQG5EPKSB","citationType":"submission","authors":["Kubota M.","Matsuura Y.","Sakai S.","Katsube Y."],"publicationDate":"FEB-1993","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CALCIUM IONS"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X59042","properties":[{"key":"ProteinId","value":"CAA41770.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X59043","properties":[{"key":"ProteinId","value":"CAA41771.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X59044","properties":[{"key":"ProteinId","value":"CAA41772.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S26588","properties":[{"key":"EntryName","value":"ALBSXF"}]},{"database":"PDB","id":"1CYG","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A=32-711"}]},{"database":"AlphaFoldDB","id":"P31797","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"P31797","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P31797","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"CBM20","properties":[{"key":"FamilyName","value":"Carbohydrate-Binding Module Family 20"}]},{"database":"CAZy","id":"GH13","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 13"}]},{"database":"BRENDA","id":"2.4.1.19","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"P31797","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004556","properties":[{"key":"GoTerm","value":"F:alpha-amylase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043169","properties":[{"key":"GoTerm","value":"F:cation binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043895","properties":[{"key":"GoTerm","value":"F:cyclomaltodextrin glucanotransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:2001070","properties":[{"key":"GoTerm","value":"F:starch binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd11320","properties":[{"key":"EntryName","value":"AmyAc_AmyMalt_CGTase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05807","properties":[{"key":"EntryName","value":"CBM20_CGTase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00604","properties":[{"key":"EntryName","value":"IPT_CGTD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.10:FF:000552","properties":[{"key":"EntryName","value":"Related to glucoamylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1180","properties":[{"key":"EntryName","value":"Golgi alpha-mannosidase II"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR006048","properties":[{"key":"EntryName","value":"A-amylase/branching_C"}]},{"database":"InterPro","id":"IPR031319","properties":[{"key":"EntryName","value":"A-amylase_C"}]},{"database":"InterPro","id":"IPR006046","properties":[{"key":"EntryName","value":"Alpha_amylase"}]},{"database":"InterPro","id":"IPR013784","properties":[{"key":"EntryName","value":"Carb-bd-like_fold"}]},{"database":"InterPro","id":"IPR002044","properties":[{"key":"EntryName","value":"CBM20"}]},{"database":"InterPro","id":"IPR006047","properties":[{"key":"EntryName","value":"GH13_cat_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR013780","properties":[{"key":"EntryName","value":"Glyco_hydro_b"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR014756","properties":[{"key":"EntryName","value":"Ig_E-set"}]},{"database":"InterPro","id":"IPR002909","properties":[{"key":"EntryName","value":"IPT_dom"}]},{"database":"PANTHER","id":"PTHR10357:SF215","properties":[{"key":"EntryName","value":"ALPHA-AMYLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10357","properties":[{"key":"EntryName","value":"ALPHA-AMYLASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00128","properties":[{"key":"EntryName","value":"Alpha-amylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02806","properties":[{"key":"EntryName","value":"Alpha-amylase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00686","properties":[{"key":"EntryName","value":"CBM_20"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01833","properties":[{"key":"EntryName","value":"TIG"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00110","properties":[{"key":"EntryName","value":"ALPHAAMYLASE"}]},{"database":"SMART","id":"SM00642","properties":[{"key":"EntryName","value":"Aamy"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00632","properties":[{"key":"EntryName","value":"Aamy_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01065","properties":[{"key":"EntryName","value":"CBM_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81296","properties":[{"key":"EntryName","value":"E set domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51011","properties":[{"key":"EntryName","value":"Glycosyl hydrolase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49452","properties":[{"key":"EntryName","value":"Starch-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51166","properties":[{"key":"EntryName","value":"CBM20"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRRWLSLVLSMSFVFSAIFIVSDTQKVTVEAAGNLNKVNFTSDVVYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYCGGDWQGIINKINDGYLTDMGVTAIWISQPVENVFSVMNDASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGTLLGGYTNDANMYFHHNGGTTFSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNHDMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMSSFNKNTRAYQVIQKLSSLRRNNPALAYGDTEQRWINGDVYVYERQFGKDVVLVAVNRSSSSNYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGSVNAFDLGPGEVGVWAYSATESTPIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYDNFEVLTNDQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESGSNHVYTTPTNTTGKIIVDWQN","length":711,"molWeight":78923,"crc64":"5F9F71FF01C2CC60","md5":"F91AA190E8E6AA52C34809118347CE21"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":2,"Region":6,"Active site":2,"Binding site":18,"Site":1,"Disulfide bond":1,"Sequence conflict":1,"Beta strand":40,"Helix":23,"Turn":5},"uniParcId":"UPI0000127415"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q09LX1","uniProtkbId":"AXE2_GEOSE","entryAudit":{"firstPublicDate":"2015-10-14","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2006-10-17","entryVersion":64,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ABI49953.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21994937"}],"value":"Acetylxylan esterase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"3.1.1.72"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24531461"}],"value":"Acetyl-xylooligosaccharide esterase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21994937"}],"value":"axe2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"Acetylxylan esterase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Cleaves acetyl side groups from the xylose backbone units of the hemicellulolytic polymer xylan and xylo-oligosaccharides. Hydrolyzes about 20%-30% of the available acetyl groups on fully acetylated birch wood xylan. Completely deacetylates xylobiose peracetate (fully acetylated), and is active on both the alpha- and beta-forms of the sugar. Also hydrolyzes fully acetylated methyl-beta-D-xylopyranoside and methyl-beta-D-glucopyranoside, and the synthetic substrates 2-naphthyl acetate, 4-nitrophenyl acetate, 4-methylumbelliferyl acetate, and phenyl acetate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Deacetylation of xylans and xylo-oligosaccharides.","ecNumber":"3.1.1.72","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":7.0,"unit":"mM","substrate":"phenyl acetate (at pH 6.0 and 30 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}]},{"constant":9.0,"unit":"mM","substrate":"2-naphtyl acetate (at pH 6.0 and 30 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}]},{"constant":3.0,"unit":"mM","substrate":"4-methylumbelliferyl acetate (at pH 6.0 and 30 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}]},{"constant":27.0,"unit":"mM","substrate":"4-nitrophenyl acetate (at pH 6.0 and 30 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"kcat is 77 sec(-1) with phenyl acetate as substrate. kcat is 190 sec(-1) with 2-naphtyl acetate as substrate. kcat is 123 sec(-1) with 4-methylumbelliferyl acetate as substrate. kcat is 31 sec(-1) with 4-nitrophenyl acetate as substrate (at pH 6.0 and 30 degrees Celsius)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"Optimum pH is 7.1-9.2."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"Optimum temperature is 50-60 degrees Celsius. Is stable at 60 degrees Celsius and loses most of its activity at 70 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24531461"}],"value":"Homooctamer, presenting a unique donut-shaped quaternary structure built of two staggered tetrameric rings. The eight active sites are organized in four closely situated pairs, which face the relatively wide internal cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21994937"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"value":"Up-regulated by xylose"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the 'GDSL' lipolytic enzyme family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Acetylxylan esterase","featureId":"PRO_0000434101"},{"type":"Active site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21994937"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24531461"}]},{"type":"Active site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21994937"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24531461"}]},{"type":"Active site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21994937"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24531461"}]},{"type":"Site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24531461"}]},{"type":"Site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24531461"}]},{"type":"Mutagenesis","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Loss of catalytic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Significant reduction in catalytic activity and modification of the quaternary structure as a homodimer; when associated with P-190.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24699743"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Significant reduction in catalytic activity and modification of the quaternary structure as a homodimer; when associated with F-184.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24699743"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["P"]}},{"type":"Mutagenesis","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"Loss of catalytic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Loss of catalytic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21994937"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Turn","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Beta strand","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4JHL"}]},{"type":"Beta strand","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Beta strand","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Beta strand","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Beta strand","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Beta strand","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]},{"type":"Helix","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5BN1"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"id":"KW-0719","category":"Molecular function","name":"Serine esterase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BGR5E3QDLL7H2","citationType":"submission","authors":["Shoham Y.","Gat O.","Shulami S.","Zaide G.","Zolotnitsky G.","Langut Y."],"title":"Hemicellulose utilization cluster in Geobacillus stearothermophilus strain T-6.","publicationDate":"JUL-2006","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"21994937","citationType":"journal article","authors":["Alalouf O.","Balazs Y.","Volkinshtein M.","Grimpel Y.","Shoham G.","Shoham Y."],"citationCrossReferences":[{"database":"PubMed","id":"21994937"},{"database":"DOI","id":"10.1074/jbc.m111.301051"}],"title":"A new family of carbohydrate esterases is represented by a GDSL hydrolase/acetylxylan esterase from Geobacillus stearothermophilus.","publicationDate":"2011","journal":"J. Biol. Chem.","firstPage":"41993","lastPage":"42001","volume":"286"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOPHYSICOCHEMICAL PROPERTIES","INDUCTION","PATHWAY","MUTAGENESIS OF SER-15; ASP-191 AND HIS-194","CATALYTIC MECHANISM","ACTIVE SITE"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"23545652","citationType":"journal article","authors":["Lansky S.","Alalouf O.","Solomon V.","Alhassid A.","Govada L.","Chayen N.E.","Chayan N.E.","Belrhali H.","Shoham Y.","Shoham G."],"citationCrossReferences":[{"database":"PubMed","id":"23545652"},{"database":"DOI","id":"10.1107/s1744309113004260"}],"title":"Crystallization and preliminary crystallographic analysis of Axe2, an acetylxylan esterase from Geobacillus stearothermophilus.","publicationDate":"2013","journal":"Acta Crystallogr. F","firstPage":"430","lastPage":"434","volume":"69"},"referencePositions":["CRYSTALLIZATION"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"24699743","citationType":"journal article","authors":["Lansky S.","Alalouf O.","Salama R.","Dvir H.","Shoham Y.","Shoham G."],"citationCrossReferences":[{"database":"PubMed","id":"24699743"},{"database":"DOI","id":"10.1107/s2053230x14004129"}],"title":"Preliminary crystallographic analysis of a double mutant of the acetyl xylo-oligosaccharide esterase Axe2 in its dimeric form.","publicationDate":"2014","journal":"Acta Crystallogr. F","firstPage":"476","lastPage":"481","volume":"70"},"referencePositions":["CRYSTALLIZATION","MUTAGENESIS OF TYR-184 AND TRP-190"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"CI-B8VGRFBG7UK9U","citationType":"submission","authors":["Lansky S.","Alalouf O.","Solomon V.","Alhassid A.","Belrahli H.","Govada L.","Chayan N.E.","Shoham Y.","Shoham G."],"title":"To be published.","publicationDate":"MAR-2013","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANTS ALA-191 AND ALA-194"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"24531461","citationType":"journal article","authors":["Lansky S.","Alalouf O.","Solomon H.V.","Alhassid A.","Govada L.","Chayen N.E.","Belrhali H.","Shoham Y.","Shoham G."],"citationCrossReferences":[{"database":"PubMed","id":"24531461"},{"database":"DOI","id":"10.1107/s139900471302840x"}],"title":"A unique octameric structure of Axe2, an intracellular acetyl-xylooligosaccharide esterase from Geobacillus stearothermophilus.","publicationDate":"2014","journal":"Acta Crystallogr. D","firstPage":"261","lastPage":"278","volume":"70"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANT ALA-15","SUBUNIT","ACTIVE SITE"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":7,"citation":{"id":"CI-45GQMSSC8U2KT","citationType":"submission","authors":["Lansky S.","Alalouf O.","Solomon H.V.","Belrhali H.","Shoham Y.","Shoham G."],"publicationDate":"JAN-2014","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANTS ALA-55 AND ILE-190"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"DQ868502","properties":[{"key":"ProteinId","value":"ABI49953.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"3W7V","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.85 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"4JHL","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"4JJ4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.13 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"4JJ6","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"4JKO","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"4OAO","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.05 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"4OAP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.93 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"PDB","id":"5BN1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A/B=1-219"}]},{"database":"AlphaFoldDB","id":"Q09LX1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q09LX1","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.1.1.72","properties":[{"key":"OrganismId","value":"623"}]},{"database":"UniPathway","id":"UPA00114","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q09LX1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0046555","properties":[{"key":"GoTerm","value":"F:acetylxylan esterase activity"},{"key":"GoEvidenceType","value":"IDA:CACAO"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"21994937"}]},{"database":"GO","id":"GO:0004622","properties":[{"key":"GoTerm","value":"F:phosphatidylcholine lysophospholipase A1 activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045493","properties":[{"key":"GoTerm","value":"P:xylan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd01834","properties":[{"key":"EntryName","value":"SGNH_hydrolase_like_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1110","properties":[{"key":"EntryName","value":"SGNH hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051532","properties":[{"key":"EntryName","value":"Ester_Hydrolysis_Enzymes"}]},{"database":"InterPro","id":"IPR013830","properties":[{"key":"EntryName","value":"SGNH_hydro"}]},{"database":"InterPro","id":"IPR036514","properties":[{"key":"EntryName","value":"SGNH_hydro_sf"}]},{"database":"PANTHER","id":"PTHR30383:SF5","properties":[{"key":"EntryName","value":"SGNH HYDROLASE-TYPE ESTERASE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30383","properties":[{"key":"EntryName","value":"THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13472","properties":[{"key":"EntryName","value":"Lipase_GDSL_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52266","properties":[{"key":"EntryName","value":"SGNH hydrolase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIGSGEKLLFIGDSITDCGRARPEGEGSFGALGTGYVAYVVGLLQAVYPELGIRVVNKGISGNTVRDLKARWEEDVIAQKPDWVSIMIGINDVWRQYDLPFMKEKHVYLDEYEATLRSLVLETKPLVKGIILMTPFYIEGNEQDPMRRTMDQYGRVVKQIAEETNSLFVDTQAAFNEVLKTLYPAALAWDRVHPSVAGHMILARAFLREIGFEWVRSR","length":219,"molWeight":24772,"crc64":"A3F18C97F5F69E32","md5":"E2256FB0D8D82B5E3C2D513676323E06"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":3,"Site":2,"Mutagenesis":5,"Beta strand":7,"Helix":14,"Turn":1},"uniParcId":"UPI0000DF0D20"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q09LY5","uniProtkbId":"AGUA_GEOSE","entryAudit":{"firstPublicDate":"2013-05-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2006-10-17","entryVersion":78,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10089319"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10368143"}],"value":"Alpha-glucuronidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}],"value":"3.2.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10089319"}],"value":"Alpha-D-glucuronidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10089319"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10368143"}],"value":"aguA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}],"value":"Alpha-glucuronidase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose (PubMed:11358519). It catalyzes the cleavage of the alpha-1,2-glycosidic bond between 4-O-methyl-D-glucuronic acid (MeGlcA) and short xylooligosaccharides, which are the main products of the enzymatic hydrolysis of xylan by xylanases, releasing 4-O-methylglucuronic acid (PubMed:11358519). It can hydrolyze the small xylooligosaccharide aldotetraouronic acid (2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylotriose or MeGlcAXyl3) to xylotriose and 4-O-methylglucuronic acid (PubMed:11358519, PubMed:14573597). Has no detectable activity either for the natural polymers, birchwood xylan and 4-O-methyl-D-glucurono-D-xylan, or for the synthetic compounds, pNP-alpha-D-glucopyranoside and pNP-beta-D-glucopyranoside (PubMed:11358519)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-O-methyl-alpha-D-glucuronosyl-(1->2)-beta-D-xylosyl-(1->4)-beta-D-xylosyl-(1->4)-beta-D-xylose + H2O = beta-D-xylotriose + 4-O-methyl-beta-D-glucuronate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:84887"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:62797"},{"database":"ChEBI","id":"CHEBI:234000"},{"database":"ChEBI","id":"CHEBI:234015"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:84888"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"value":"The metal cations Ni(2+), K(+) and Zn(2+) show some inhibition of the activity, and Ag(+), Hg(2+) and Cu(2+) show very significant inhibition even at relatively low ion concentrations"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":42.0,"unit":"umol/min/ug","enzyme":"enzyme with aldotetraouronic acid as substrate (at 55 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}]}],"michaelisConstants":[{"constant":0.2,"unit":"mM","substrate":"aldotetraouronic acid (at 55 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"value":"Optimum pH is 5.5-6. It retains about 40% of its activity at pH 4.5 and 7.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"value":"Optimum temperature is 65 degrees Celsius. The enzyme is stable up to 70 degrees Celsius and loses 70% of its activity at 75 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10089319"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11358519"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 67 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"Alpha-glucuronidase","featureId":"PRO_0000422175"},{"type":"Active site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}]},{"type":"Active site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}]},{"type":"Active site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}]},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Binding site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:234000"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"}],"ligand":{"name":"4-O-methyl-beta-D-glucuronate","id":"ChEBI:CHEBI:234000"}},{"type":"Mutagenesis","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Strong decrease in glucuronidase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"Relatively low glucuronidase activity, but shows binding to the substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"Loss of glucuronidase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"14-fold decrease in glucuronidase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14573597"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Loss of glucuronidase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"Strong decrease in glucuronidase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358519"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MQR"}]},{"type":"Helix","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":476,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":511,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1MQR"}]},{"type":"Turn","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":526,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":532,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":538,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Beta strand","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":551,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":557,"modifier":"EXACT"},"end":{"value":559,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":563,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":569,"modifier":"EXACT"},"end":{"value":576,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":578,"modifier":"EXACT"},"end":{"value":580,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":583,"modifier":"EXACT"},"end":{"value":585,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":586,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":604,"modifier":"EXACT"},"end":{"value":627,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Turn","location":{"start":{"value":628,"modifier":"EXACT"},"end":{"value":631,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]},{"type":"Helix","location":{"start":{"value":635,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1K9F"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"id":"KW-0858","category":"Biological process","name":"Xylan degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"10368143","citationType":"journal article","authors":["Shulami S.","Gat O.","Sonenshein A.L.","Shoham Y."],"citationCrossReferences":[{"database":"PubMed","id":"10368143"},{"database":"DOI","id":"10.1128/jb.181.12.3695-3704.1999"}],"title":"The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6.","publicationDate":"1999","journal":"J. Bacteriol.","firstPage":"3695","lastPage":"3704","volume":"181"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"11358519","citationType":"journal article","authors":["Zaide G.","Shallom D.","Shulami S.","Zolotnitsky G.","Golan G.","Baasov T.","Shoham G.","Shoham Y."],"citationCrossReferences":[{"database":"PubMed","id":"11358519"},{"database":"DOI","id":"10.1046/j.1432-1327.2001.02193.x"}],"title":"Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6.","publicationDate":"2001","journal":"Eur. J. Biochem.","firstPage":"3006","lastPage":"3016","volume":"268"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOPHYSICOCHEMICAL PROPERTIES","ACTIVITY REGULATION","SUBUNIT","MUTAGENESIS OF GLU-158; GLU-285; ASP-364; GLU-386; GLU-392 AND GLU-510"],"referenceComments":[{"value":"T-6","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"10089319","citationType":"journal article","authors":["Teplitsky A.","Shulami S.","Moryles S.","Zaide G.","Shoham Y.","Shoham G."],"citationCrossReferences":[{"database":"PubMed","id":"10089319"},{"database":"DOI","id":"10.1107/s0907444998012918"}],"title":"Crystallization and preliminary X-ray analysis of alpha-D-glucuronidase from Bacillus stearothermophilus T-6.","publicationDate":"1999","journal":"Acta Crystallogr. D","firstPage":"869","lastPage":"872","volume":"55"},"referencePositions":["SUBUNIT","CRYSTALLIZATION"]},{"referenceNumber":4,"citation":{"id":"14573597","citationType":"journal article","authors":["Golan G.","Shallom D.","Teplitsky A.","Zaide G.","Shulami S.","Baasov T.","Stojanoff V.","Thompson A.","Shoham Y.","Shoham G."],"citationCrossReferences":[{"database":"PubMed","id":"14573597"},{"database":"DOI","id":"10.1074/jbc.m310098200"}],"title":"Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications.","publicationDate":"2004","journal":"J. Biol. Chem.","firstPage":"3014","lastPage":"3024","volume":"279"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF WILD-TYPE; MUTANT GLN-386 AND MUTANT ASN-285 IN COMPLEXES WITH 4-O-METHYL-GLUCURONIC ACID AND ALDOTETRAURONIC ACID","FUNCTION","CATALYTIC ACTIVITY","ACTIVE SITE","REACTION MECHANISM","SUBUNIT","MUTAGENESIS OF GLU-285 AND GLU-386"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9E"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1K9F"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MQP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1MQR"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"DQ868502","properties":[{"key":"ProteinId","value":"ABI49940.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"1K9E","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.85 A"},{"key":"Chains","value":"A=1-679"}]},{"database":"PDB","id":"1K9F","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A=1-679"}]},{"database":"PDB","id":"1MQP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=1-679"}]},{"database":"PDB","id":"1MQR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=1-679"}]},{"database":"AlphaFoldDB","id":"Q09LY5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q09LY5","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH67","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 67"}]},{"database":"BRENDA","id":"3.2.1.139","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"Q09LY5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046559","properties":[{"key":"GoTerm","value":"F:alpha-glucuronidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033939","properties":[{"key":"GoTerm","value":"F:xylan alpha-1,2-glucuronosidase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11358519"}]},{"database":"GO","id":"GO:2000886","properties":[{"key":"GoTerm","value":"P:glucuronoxylan catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11358519"}]},{"database":"FunFam","id":"3.30.379.10:FF:000006","properties":[{"key":"EntryName","value":"Extracellular xylan exo-alpha-(1->2)-glucuronosidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.80:FF:000096","properties":[{"key":"EntryName","value":"Xylan alpha-1,2-glucuronidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1330.10:FF:000001","properties":[{"key":"EntryName","value":"Xylan alpha-1,2-glucuronidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1330.10","properties":[{"key":"EntryName","value":"Alpha-glucuronidase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.379.10","properties":[{"key":"EntryName","value":"Chitobiase/beta-hexosaminidase domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR037054","properties":[{"key":"EntryName","value":"A-glucoronidase_C_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR011395","properties":[{"key":"EntryName","value":"Glyco_hydro_67_aGlcAse"}]},{"database":"InterPro","id":"IPR005154","properties":[{"key":"EntryName","value":"Glyco_hydro_67_aGlcAse_N"}]},{"database":"InterPro","id":"IPR011099","properties":[{"key":"EntryName","value":"Glyco_hydro_67_C"}]},{"database":"InterPro","id":"IPR011100","properties":[{"key":"EntryName","value":"Glyco_hydro_67_cat"}]},{"database":"InterPro","id":"IPR029018","properties":[{"key":"EntryName","value":"Hex-like_dom2"}]},{"database":"PANTHER","id":"PTHR39207","properties":[{"key":"EntryName","value":"ALPHA-GLUCURONIDASE A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39207:SF1","properties":[{"key":"EntryName","value":"ALPHA-GLUCURONIDASE A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07477","properties":[{"key":"EntryName","value":"Glyco_hydro_67C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07488","properties":[{"key":"EntryName","value":"Glyco_hydro_67M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03648","properties":[{"key":"EntryName","value":"Glyco_hydro_67N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF029900","properties":[{"key":"EntryName","value":"Alpha-glucuronds"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55545","properties":[{"key":"EntryName","value":"beta-N-acetylhexosaminidase-like domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAGYEPCWLRYERKDQYSRLRFEEIVAKRTSPIFQAVVEELQKGLRSMMEIEPQVVQEVNETANSIWLGTLEDEEFERPLEGTLVHPEGYVIRSDVDDGPFRIYIIGKTDAGVLYGVFHFLRLLQMGENIAQLSIIEQPKNRLRMINHWDNMDGSIERGYAGRSIFFVDDQFVKQNQRIKDYARLLASVGINAISINNVNVHKTETKLITDHFLPDVAEVADIFRTYGIKTFLSINYASPIEIGGLPTADPLDPEVRRWWKETAKRIYQYIPDFGGFVVKADSEFRPGPFTYGRDHAEGANMLAEALAPFGGLVIWRCFVYNCQQDWRDRTTDRAKAAYDHFKPLDGQFRENVILQIKNGPMDFQVREPVSPLFGAMPKTNQMMEVQITQEYTGQQKHLCFLIPQWKEVLDFDTYAKGKGSEVKKVIDGSLFDYRYSGIAGVSNIGSDPNWTGHTLAQANLYGFGRLAWNPDLSAEEIANEWVVQTFGDDSQVVETISWMLLSSWRIYENYTSPLGVGWMVNPGHHYGPNVDGYEYSHWGTYHYADRDGIGVDRTVATGTGYTAQYFPENAAMYESLDTCPDELLLFFHHVPYTHRLHSGETVIQHIYNTHFEGVEQAKQLRKRWEQLKGKIDEKRYHDVLERLTIQVEHAKEWRDVINTYFYRKSGIDDQYGRKIYR","length":679,"molWeight":78484,"crc64":"275785B40B64DEC4","md5":"663FE235F3AB6B23DE1984B1BF8581E3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":3,"Binding site":8,"Mutagenesis":6,"Beta strand":22,"Helix":26,"Turn":9},"uniParcId":"UPI00000AE7C0"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q53389","uniProtkbId":"AMAB2_GEOSE","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":99,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22904279"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7764340"}],"value":"N-carbamoyl-L-amino acid amidohydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"value":"3.5.1.87"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22904279"}],"value":"BsLcar"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22904279"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7764340"}],"value":"L-N-carbamoylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7764340"}],"value":"amaB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P37113"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"value":"Catalyzes the hydrolysis of N-carbamoyl-L-alpha-amino acids to free L-alpha-amino acids (PubMed:22904279). Is strictly L-specific since it is inactive toward N-carbamoyl-D-alpha-amino acids (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N-carbamoyl-L-alpha-amino acid + H2O + 2 H(+) = an L-alpha-amino acid + NH4(+) + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17581"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:58865"},{"database":"ChEBI","id":"CHEBI:59869"}],"ecNumber":"3.5.1.87","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17582"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22904279"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-carbamoyl-L-methionine + H2O + 2 H(+) = L-methionine + NH4(+) + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:72783"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:137116"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:72784"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22904279"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}},{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}},{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"value":"Requires divalent metal cations for activity. Binds 2 divalent metal cations per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q53389","intActId":"EBI-6421173"},"interactantTwo":{"uniProtKBAccession":"Q53389","geneName":"amaB","intActId":"EBI-6421173"},"numberOfExperiments":3,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase M20 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"N-carbamoyl-L-amino acid amidohydrolase","featureId":"PRO_0000061953"},{"type":"Region","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Involved in dimerization","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3N5F"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240","label":"1"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3N5F"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240","label":"1"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240","label":"2"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240","label":"2"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3N5F"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240","label":"1"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58865"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"an N-carbamoyl-L-alpha-amino acid","id":"ChEBI:CHEBI:58865"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58865"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"an N-carbamoyl-L-alpha-amino acid","id":"ChEBI:CHEBI:58865"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58865"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"an N-carbamoyl-L-alpha-amino acid","id":"ChEBI:CHEBI:58865"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58865"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"an N-carbamoyl-L-alpha-amino acid","id":"ChEBI:CHEBI:58865"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58865"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"an N-carbamoyl-L-alpha-amino acid","id":"ChEBI:CHEBI:58865"}},{"type":"Binding site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6DTN4"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240","label":"2"}},{"type":"Site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Necessary for dimerization","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}]},{"type":"Mutagenesis","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Loss of activity and impaired dimerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22904279"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Helix","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Turn","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Turn","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Turn","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Turn","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Turn","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Turn","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Beta strand","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]},{"type":"Helix","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3N5F"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0533","category":"Ligand","name":"Nickel"}],"references":[{"referenceNumber":1,"citation":{"id":"7764340","citationType":"journal article","authors":["Mukohara Y.","Ishikawa T.","Watabe K.","Nakamura H."],"citationCrossReferences":[{"database":"PubMed","id":"7764340"},{"database":"DOI","id":"10.1271/bbb.57.1935"}],"title":"Molecular cloning and sequencing of the gene for a thermostable N-carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS1122A.","publicationDate":"1993","journal":"Biosci. Biotechnol. Biochem.","firstPage":"1935","lastPage":"1937","volume":"57"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"NS1122A","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"22904279","citationType":"journal article","authors":["Martinez-Rodriguez S.","Garcia-Pino A.","Las Heras-Vazquez F.J.","Clemente-Jimenez J.M.","Rodriguez-Vico F.","Garcia-Ruiz J.M.","Loris R.","Gavira J.A."],"citationCrossReferences":[{"database":"PubMed","id":"22904279"},{"database":"DOI","id":"10.1128/jb.01056-12"}],"title":"Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.","publicationDate":"2012","journal":"J. Bacteriol.","firstPage":"5759","lastPage":"5768","volume":"194"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH COBALT","FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF HIS-225; ARG-234; THR-261; ASN-273; ASP-284 AND ARG-286","SUBUNIT","COFACTOR"],"referenceComments":[{"value":"CECT43","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"S67784","properties":[{"key":"ProteinId","value":"AAC60456.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JN0885","properties":[{"key":"EntryName","value":"JN0885"}]},{"database":"PDB","id":"3N5F","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.75 A"},{"key":"Chains","value":"A/B=1-408"}]},{"database":"AlphaFoldDB","id":"Q53389","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q53389","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.5.1.87","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"Q53389","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0050897","properties":[{"key":"GoTerm","value":"F:cobalt ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22904279"}]},{"database":"GO","id":"GO:0016813","properties":[{"key":"GoTerm","value":"F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IPI:IntAct"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"22904279"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22904279"}]},{"database":"GO","id":"GO:0050538","properties":[{"key":"GoTerm","value":"F:N-carbamoyl-L-amino-acid hydrolase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22904279"}]},{"database":"CDD","id":"cd03884","properties":[{"key":"EntryName","value":"M20_bAS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.10:FF:000044","properties":[{"key":"EntryName","value":"Allantoate amidohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.360","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.10","properties":[{"key":"EntryName","value":"Zn peptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036264","properties":[{"key":"EntryName","value":"Bact_exopeptidase_dim_dom"}]},{"database":"InterPro","id":"IPR010158","properties":[{"key":"EntryName","value":"HyuC"}]},{"database":"InterPro","id":"IPR002933","properties":[{"key":"EntryName","value":"Peptidase_M20"}]},{"database":"InterPro","id":"IPR011650","properties":[{"key":"EntryName","value":"Peptidase_M20_dimer"}]},{"database":"NCBIfam","id":"TIGR01879","properties":[{"key":"EntryName","value":"hydantase"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006771","properties":[{"key":"EntryName","value":"PRK09290.1-5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32494","properties":[{"key":"EntryName","value":"ALLANTOATE DEIMINASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32494:SF19","properties":[{"key":"EntryName","value":"ALLANTOATE DEIMINASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07687","properties":[{"key":"EntryName","value":"M20_dimer"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01546","properties":[{"key":"EntryName","value":"Peptidase_M20"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001235","properties":[{"key":"EntryName","value":"Amidase_carbamoylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55031","properties":[{"key":"EntryName","value":"Bacterial exopeptidase dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53187","properties":[{"key":"EntryName","value":"Zn-dependent exopeptidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIQGERLWQRLMELGEVGKQPSGGVTRLSFTAEERRAKDLVASYMREAGLFVYEDAAGNLIGRKEGTNPDATVVLVGSHLDSVYNGGCFDGPLGVLAGVEVVQTMNEHGVVTHHPIEVVAFTDEEGARFRFGMIGSRAMAGTLPPEALECRDAEGISLAEAMKQAGLDPDRLPQAARKPGTVKAYVELHIEQGRVLEETGLPVGIVTGIAGLIWVKFTIEGKAEHAGATPMSLRRDPMAAAAQIIIVIEEEARRTGTTVGTVGQLHVYPGGINVIPERVEFVLDLRDLKAEVRDQVWKAIAVRAETIAKERNVRVTTERLQEMPPVLCSDEVKRAAEAACQKLGYPSFWLPSGAAHDSVQLAPICPIGMIFVRSQDGVSHSPAEWSTKEDCAAGAEVLYHTVWQLAQGE","length":409,"molWeight":44249,"crc64":"332515C62A1A2F31","md5":"23E858161781C63E367EAE7AF0A66FBC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"INTERACTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Binding site":11,"Site":1,"Mutagenesis":6,"Helix":13,"Turn":6,"Beta strand":14},"uniParcId":"UPI0000125945"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9X4C9","uniProtkbId":"DNAB_GEOSE","entryAudit":{"firstPublicDate":"2024-07-24","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1999-11-01","entryVersion":144,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10095066"}],"value":"Replicative DNA helicase DnaB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10625492"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12235389"}],"value":"5.6.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA 5'-3' helicase DnaB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10095066"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAD20314.1"}],"value":"dnaB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10625492"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17003052"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}],"value":"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable) (PubMed:23022319). Has ssDNA-stimulated ATPase activity (PubMed:10625492). DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3') (PubMed:10625492, PubMed:12235389, PubMed:23022319). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA (PubMed:17003052). Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'-adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved (PubMed:12235389, PubMed:17003052)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10095066"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10625492"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12235389"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10625492"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10625492"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15556628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17003052"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17947583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19255093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23525462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24048025"}],"value":"Homohexamer (PubMed:10625492, PubMed:17003052, PubMed:17947583, PubMed:23525462, PubMed:23022319, PubMed:24048025). Interacts with DnaG primase, as DnaB(6):DnaG(3) (PubMed:10625492, PubMed:17947583, PubMed:24048025). Interacts with the N-terminus of DnaI (shown with DnaI of B.subtilis), forms a helicase DnaB(6):DnaI(6) complex (PubMed:17003052, PubMed:19255093, PubMed:24048025). The DnaB-DnaI complex is disrupted by DnaD (DnaD and DnaI from B.subtilis) (PubMed:15556628). A stable complex DnaI(6):DnaB(6):DnaG(3) fragment can be isolated; DnaI and DnaG do not contact each other (DnaI in this complex is derived from B.subtilis) (PubMed:24048025). Forms a complex with DNA clamp loader protein tau (shown with B.subtilis HolA) tau(3):DnaB(6); a single ATP hydrolysis even is sufficient for complex formation (PubMed:23525462)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9X4C9","intActId":"EBI-6402993"},"interactantTwo":{"uniProtKBAccession":"Q9X4C9","geneName":"dnaB","intActId":"EBI-6402993"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9X4C9","intActId":"EBI-6402993"},"interactantTwo":{"uniProtKBAccession":"Q9X4D0","geneName":"dnaG","intActId":"EBI-6403005"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9X4C9","intActId":"EBI-6402993"},"interactantTwo":{"uniProtKBAccession":"P09122","geneName":"dnaX","intActId":"EBI-5243974"},"numberOfExperiments":2,"organismDiffer":true}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17947583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23022319"}],"value":"Within the hexamer the N-terminal domains (NTD) form a rigid ring, while the C-terminal domains (CTD) form a looser ring; the 2 rings stack to form a double-layered ring (PubMed:17947583). In a complex without DNA or bound nucleotides the central channel varies from 25-50 Angstroms in diameter (PubMed:17947583). The NTD interacts with the helicase-binding domain of DnaG primase (PubMed:17947583). In complex with ssDNA and an NTP analog forms a double-layered, right-handed spiral staircase with a small internal diameter; 5 of the 6 subunits bind NTP (PubMed:23022319). Closely contacts 11 nucleotides of ssDNA, the 5'-end points toward the NTD staircase (PubMed:23022319). Binding of ssDNA and NTP induces domain movements that allow the ATP-binding sites to form (PubMed:23022319)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12235389"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}],"value":"The gamma-phosphate sensor residue (Gln-362) may sense nucleotide binding/hydrolysis in the active site; it is also important in DnaG-induced stimulation of DnaB activity (PubMed:12235389, PubMed:23022319). Other possible gamma-phosphate sensor residues are Lys-216; Lys-418 and Arg-420 (PubMed:23022319)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the helicase family. DnaB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"Replicative DNA helicase DnaB","featureId":"PRO_0000460599"},{"type":"Domain","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"SF4 helicase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00596"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"N-terminal domain (NTD)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17947583"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}]},{"type":"Region","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Linker helix","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17947583"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}]},{"type":"Region","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"C-terminal domain (CTD)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17947583"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}]},{"type":"Active site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12235389"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}]},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:9160"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ssDNA","id":"ChEBI:CHEBI:9160"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:9160"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ssDNA","id":"ChEBI:CHEBI:9160"}},{"type":"Binding site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:9160"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ssDNA","id":"ChEBI:CHEBI:9160"}},{"type":"Binding site","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23022319"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"Gamma-phosphate sensor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12235389"}]},{"type":"Mutagenesis","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"Loss of helicase activity, reduced ATPase activity, still forms homohexamers, ATPase not activated by DnaG primase, still interacts with DnaG, almost complete loss of ssDNA-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Loss of helicase and ATPase activity, still interacts with DnaG, complete loss of ssDNA-binding. No longer forms a complex with DNA clamp loader subunit tau.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23525462"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Loss of helicase activity, reduced ATPase activity, ATPase partially activated by DnaG primase, 4-fold decreased ssDNA-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Loss of helicase and ATPase activity, still interacts with DnaG, 4- to 15-fold decreased ssDNA-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A","N"]}},{"type":"Mutagenesis","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"Partial loss of helicase and ATPase activities, ATPase and helicase partially activated by DnaG primase, wild-type ss- and dsDNA binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"Partial loss of helicase and ATPase activities, still forms homohexamers, ATPase and helicase not activated by DnaG primase, still interacts with DnaG, binds ss- and dsDNA in absence of nucleotide and less well in presence of nucleotide.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["K"]}},{"type":"Helix","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Turn","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Turn","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4ESV"}]},{"type":"Beta strand","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4ESV"}]},{"type":"Helix","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Helix","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4ESV"}]},{"type":"Beta strand","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Turn","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]},{"type":"Beta strand","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R6A"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0639","category":"Cellular component","name":"Primosome"}],"references":[{"referenceNumber":1,"citation":{"id":"10095066","citationType":"journal article","authors":["Bird L.E.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"10095066"},{"database":"DOI","id":"10.1016/s0167-4781(99)00024-x"}],"title":"The Bacillus stearothermophilus replicative helicase: cloning, overexpression and activity.","publicationDate":"1999","journal":"Biochim. Biophys. Acta","firstPage":"424","lastPage":"428","volume":"1444"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION AS A HELICASE"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAD20314.1"}]},{"referenceNumber":2,"citation":{"id":"10625492","citationType":"journal article","authors":["Bird L.E.","Pan H.","Soultanas P.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"10625492"},{"database":"DOI","id":"10.1021/bi9918801"}],"title":"Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus.","publicationDate":"2000","journal":"Biochemistry","firstPage":"171","lastPage":"182","volume":"39"},"referencePositions":["PROTEIN SEQUENCE OF 1-4; 151-158 AND 451-454","FUNCTION AS A HELICASE","FUNCTION AS AN ATPASE","SUBUNIT"],"referenceComments":[{"value":"ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"12235389","citationType":"journal article","authors":["Soultanas P.","Wigley D.B."],"citationCrossReferences":[{"database":"PubMed","id":"12235389"},{"database":"DOI","id":"10.1093/nar/gkf527"}],"title":"Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus.","publicationDate":"2002","journal":"Nucleic Acids Res.","firstPage":"4051","lastPage":"4060","volume":"30"},"referencePositions":["FUNCTION AS A HELICASE","FUNCTION AS AN ATPASE","POSSIBLE ACTIVE SITE","SSDNA-BINDING","MUTAGENESIS OF LYS-216; THR-217; GLU-241; ASP-320 AND GLN-362"]},{"referenceNumber":4,"citation":{"id":"15556628","citationType":"journal article","authors":["Turner I.J.","Scott D.J.","Allen S.","Roberts C.J.","Soultanas P."],"citationCrossReferences":[{"database":"PubMed","id":"15556628"},{"database":"DOI","id":"10.1016/j.febslet.2004.10.051"}],"title":"The Bacillus subtilis DnaD protein: a putative link between DNA remodeling and initiation of DNA replication.","publicationDate":"2004","journal":"FEBS Lett.","firstPage":"460","lastPage":"464","volume":"577"},"referencePositions":["SUBUNIT"]},{"referenceNumber":5,"citation":{"id":"17003052","citationType":"journal article","authors":["Ioannou C.","Schaeffer P.M.","Dixon N.E.","Soultanas P."],"citationCrossReferences":[{"database":"PubMed","id":"17003052"},{"database":"DOI","id":"10.1093/nar/gkl690"}],"title":"Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.","publicationDate":"2006","journal":"Nucleic Acids Res.","firstPage":"5247","lastPage":"5258","volume":"34"},"referencePositions":["SUBUNIT","DNA-BINDING"]},{"referenceNumber":6,"citation":{"id":"19255093","citationType":"journal article","authors":["Loscha K.V.","Jaudzems K.","Ioannou C.","Su X.C.","Hill F.R.","Otting G.","Dixon N.E.","Liepinsh E."],"citationCrossReferences":[{"database":"PubMed","id":"19255093"},{"database":"DOI","id":"10.1093/nar/gkp092"}],"title":"A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader.","publicationDate":"2009","journal":"Nucleic Acids Res.","firstPage":"2395","lastPage":"2404","volume":"37"},"referencePositions":["SUBUNIT"]},{"referenceNumber":7,"citation":{"id":"17947583","citationType":"journal article","authors":["Bailey S.","Eliason W.K.","Steitz T.A."],"citationCrossReferences":[{"database":"PubMed","id":"17947583"},{"database":"DOI","id":"10.1126/science.1147353"}],"title":"Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase.","publicationDate":"2007","journal":"Science","firstPage":"459","lastPage":"463","volume":"318"},"referencePositions":["X-RAY CRYSTALLOGRAPHY ALONE","X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH C-TERMINUS OF DNAG","INTERACTION WITH DNAG","DOMAIN"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"2R6A"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2R6C"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2R6D"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2R6E"}]},{"referenceNumber":8,"citation":{"id":"23525462","citationType":"journal article","authors":["Afonso J.P.","Chintakayala K.","Suwannachart C.","Sedelnikova S.","Giles K.","Hoyes J.B.","Soultanas P.","Rafferty J.B.","Oldham N.J."],"citationCrossReferences":[{"database":"PubMed","id":"23525462"},{"database":"DOI","id":"10.1093/nar/gkt173"}],"title":"Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase.","publicationDate":"2013","journal":"Nucleic Acids Res.","firstPage":"5115","lastPage":"5126","volume":"41"},"referencePositions":["SUBUNIT","MUTAGENESIS OF THR-217"]},{"referenceNumber":9,"citation":{"id":"23022319","citationType":"journal article","authors":["Itsathitphaisarn O.","Wing R.A.","Eliason W.K.","Wang J.","Steitz T.A."],"citationCrossReferences":[{"database":"PubMed","id":"23022319"},{"database":"DOI","id":"10.1016/j.cell.2012.09.014"}],"title":"The hexameric helicase DnaB adopts a nonplanar conformation during translocation.","publicationDate":"2012","journal":"Cell","firstPage":"267","lastPage":"277","volume":"151"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NTP ANALOG AND SSDNA","POSSIBLE REACTION MECHANISM","PROBABLE ACTIVE SITE","DOMAIN","DNA-BINDING"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"4ESV"}]},{"referenceNumber":10,"citation":{"id":"24048025","citationType":"journal article","authors":["Liu B.","Eliason W.K.","Steitz T.A."],"citationCrossReferences":[{"database":"PubMed","id":"24048025"},{"database":"DOI","id":"10.1038/ncomms3495"}],"title":"Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.","publicationDate":"2013","journal":"Nat. Commun.","firstPage":"2495","lastPage":"2495","volume":"4"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH DNAG AND DNAI OF B.SUBTILIS"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"4M4W"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF106032","properties":[{"key":"ProteinId","value":"AAD20314.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"2R6A","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.90 A"},{"key":"Chains","value":"A/B=1-454"}]},{"database":"PDB","id":"2R6C","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"4.00 A"},{"key":"Chains","value":"A/B/C/D/E/F=1-454"}]},{"database":"PDB","id":"2R6D","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.70 A"},{"key":"Chains","value":"A/B/C/D/E/F=1-454"}]},{"database":"PDB","id":"2R6E","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"5.02 A"},{"key":"Chains","value":"A/B=1-454"}]},{"database":"PDB","id":"4ESV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.20 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H/I/J/K/L=1-454"}]},{"database":"PDB","id":"4M4W","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"6.10 A"},{"key":"Chains","value":"A/B/C/D/E/F=1-454"}]},{"database":"PDB","id":"9P9A","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"3.50 A"},{"key":"Chains","value":"A/B/C/D/F/H=1-454"}]},{"database":"AlphaFoldDB","id":"Q9X4C9","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-71404","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9X4C9","properties":[{"key":"Description","value":"-"}]},{"database":"DIP","id":"DIP-48437N","properties":[{"key":"Description","value":"-"}]},{"database":"IntAct","id":"Q9X4C9","properties":[{"key":"Interactions","value":"3"}]},{"database":"EvolutionaryTrace","id":"Q9X4C9","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10625492"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12235389"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IPI:IntAct"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"17947583"},{"evidenceCode":"ECO:0000353","source":"PubMed","id":"18366438"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00984","properties":[{"key":"EntryName","value":"DnaB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.860.10:FF:000001","properties":[{"key":"EntryName","value":"Replicative DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000076","properties":[{"key":"EntryName","value":"Replicative DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.860.10","properties":[{"key":"EntryName","value":"DNAb Helicase, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036185","properties":[{"key":"EntryName","value":"DNA_heli_DnaB-like_N_sf"}]},{"database":"InterPro","id":"IPR007692","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB"}]},{"database":"InterPro","id":"IPR007694","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB-like_C"}]},{"database":"InterPro","id":"IPR007693","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB-like_N"}]},{"database":"InterPro","id":"IPR016136","properties":[{"key":"EntryName","value":"DNA_helicase_N/primase_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00665","properties":[{"key":"EntryName","value":"DnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004384","properties":[{"key":"EntryName","value":"dnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30153:SF2","properties":[{"key":"EntryName","value":"REPLICATIVE DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30153","properties":[{"key":"EntryName","value":"REPLICATIVE DNA HELICASE DNAB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00772","properties":[{"key":"EntryName","value":"DnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03796","properties":[{"key":"EntryName","value":"DnaB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48024","properties":[{"key":"EntryName","value":"N-terminal domain of DnaB helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00039","properties":[{"key":"EntryName","value":"DEAD_ATP_HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51199","properties":[{"key":"EntryName","value":"SF4_HELICASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSELFSERIPPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTREDEIDVLLDEADRKIMEVSQRKHSGAFKNIKDILVQTYDNIEMLHNRDGEITGIPTGFTELDRMTSGFQRSDLIIVAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQLVMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAGIYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQGSGRSKENRQQEVSEISRSLKALARELEVPVIALSQLSRSVEQRQDKRPMMSDIRESGSIEQDADIVAFLYRDDYYNKDSENKNIIEIIIAKQRNGPVGTVQLAFIKEYNKFVNLERRFDEAQIPPGA","length":454,"molWeight":50643,"crc64":"D6115B868E11BAC0","md5":"0450BE4F655084A3E64473EC4CA50AFD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"INTERACTION":3,"DOMAIN":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Region":3,"Active site":1,"Binding site":13,"Site":1,"Mutagenesis":6,"Helix":24,"Turn":3,"Beta strand":11},"uniParcId":"UPI00000AEC18"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9X519","uniProtkbId":"GPMI_GEOSE","entryAudit":{"firstPublicDate":"2003-01-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":136,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10388626"}],"value":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10388626"}],"value":"23PGA-independent"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10388626"}],"value":"BPG-independent PGAM"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10388626"}],"value":"Phosphoglyceromutase"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10388626"}],"value":"iPGM"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}],"value":"5.4.2.12"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01038"}],"value":"gpmI"},"synonyms":[{"value":"pgm"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"value":"Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15901"},{"database":"ChEBI","id":"CHEBI:58272"},{"database":"ChEBI","id":"CHEBI:58289"}],"ecNumber":"5.4.2.12","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"value":"Binds 2 manganese ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10388626"}],"value":"Could be inhibited during sporulation by acidification of the forespore, thus allowing accumulation of the spore's large depot of 3-phosphoglyceric acid"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":4.4,"unit":"mM","substrate":"3-pGA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}],"value":"Very sensitive to pH. The enzyme activity rises 25-fold between pH 6 and 8."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}],"value":"Addition of manganese increases the thermal stability."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"MASS SPECTROMETRY","method":"MALDI","molWeight":56877.0,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10764795"}],"value":"The pH sensitivity is physiologically relevant, since it allows for the regulation of iPGM activity during different parts of the developmental cycle"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the BPG-independent phosphoglycerate mutase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388626"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":511,"modifier":"EXACT"}},"description":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase","featureId":"PRO_0000212127"},{"type":"Active site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":444,"modifier":"EXACT"},"end":{"value":444,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":462,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Modified residue","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01038"}]},{"type":"Mutagenesis","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Loss of mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Loss of mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12729763"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Strong decrease in the mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Strong decrease in the mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"5-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"Loss of mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Loss of mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"5-fold decrease in the mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":462,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Strong decrease in the mutase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747010"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Beta strand","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Turn","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1EJJ"}]},{"type":"Beta strand","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Turn","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Turn","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Turn","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":444,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":467,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Beta strand","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":484,"modifier":"EXACT"},"end":{"value":486,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":487,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1O98"}]},{"type":"Helix","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1EQJ"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0749","category":"Biological process","name":"Sporulation"}],"references":[{"referenceNumber":1,"citation":{"id":"10388626","citationType":"journal article","authors":["Chander M.","Setlow P.","Lamani E.","Jedrzejas M.J."],"citationCrossReferences":[{"database":"PubMed","id":"10388626"},{"database":"DOI","id":"10.1006/jsbi.1999.4112"}],"title":"Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus.","publicationDate":"1999","journal":"J. Struct. Biol.","firstPage":"156","lastPage":"165","volume":"126"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-8","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","COFACTOR","MASS SPECTROMETRY","CRYSTALLIZATION","SUBUNIT"]},{"referenceNumber":2,"citation":{"id":"10747010","citationType":"journal article","authors":["Jedrzejas M.J.","Chander M.","Setlow P.","Krishnasamy G."],"citationCrossReferences":[{"database":"PubMed","id":"10747010"},{"database":"DOI","id":"10.1093/emboj/19.7.1419"}],"title":"Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus.","publicationDate":"2000","journal":"EMBO J.","firstPage":"1419","lastPage":"1431","volume":"19"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE AND MANGANESE","FUNCTION","MUTAGENESIS OF ASP-12; HIS-42; SER-62; HIS-66; HIS-123; HIS-125; HIS-128; ARG-261; HIS-407 AND HIS-445","COFACTOR","ACTIVE SITE","REACTION MECHANISM"]},{"referenceNumber":3,"citation":{"id":"10764795","citationType":"journal article","authors":["Jedrzejas M.J.","Chander M.","Setlow P.","Krishnasamy G."],"citationCrossReferences":[{"database":"PubMed","id":"10764795"},{"database":"DOI","id":"10.1074/jbc.m002544200"}],"title":"Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.","publicationDate":"2000","journal":"J. Biol. Chem.","firstPage":"23146","lastPage":"23153","volume":"275"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE AND MANGANESE","COFACTOR"]},{"referenceNumber":4,"citation":{"id":"12729763","citationType":"journal article","authors":["Rigden D.J.","Lamani E.","Mello L.V.","Littlejohn J.E.","Jedrzejas M.J."],"citationCrossReferences":[{"database":"PubMed","id":"12729763"},{"database":"DOI","id":"10.1016/s0022-2836(03)00350-4"}],"title":"Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling.","publicationDate":"2003","journal":"J. Mol. Biol.","firstPage":"909","lastPage":"920","volume":"328"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANT ALA-62 IN COMPLEX WITH SUBSTRATE AND MANGANESE","MUTAGENESIS OF SER-62","COFACTOR","ACTIVE SITE"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF120091","properties":[{"key":"ProteinId","value":"AAD26328.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46865","properties":[{"key":"EntryName","value":"T46865"}]},{"database":"RefSeq","id":"WP_033015095.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAIEX010000002.1"}]},{"database":"PDB","id":"1EJJ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=1-511"}]},{"database":"PDB","id":"1EQJ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=1-511"}]},{"database":"PDB","id":"1O98","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A=1-511"}]},{"database":"PDB","id":"1O99","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.65 A"},{"key":"Chains","value":"A=1-511"}]},{"database":"AlphaFoldDB","id":"Q9X519","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9X519","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB01709","properties":[{"key":"GenericName","value":"2-phospho-D-glyceric acid"}]},{"database":"DrugBank","id":"DB04510","properties":[{"key":"GenericName","value":"3-phospho-D-glyceric acid"}]},{"database":"GeneID","id":"89613288","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:AAD26328","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9800863at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"5.4.2.12","properties":[{"key":"OrganismId","value":"623"}]},{"database":"SABIO-RK","id":"Q9X519","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00186"}]},{"database":"EvolutionaryTrace","id":"Q9X519","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10388626"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10747010"}]},{"database":"GO","id":"GO:0004619","properties":[{"key":"GoTerm","value":"F:phosphoglycerate mutase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10388626"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10747010"}]},{"database":"GO","id":"GO:0006007","properties":[{"key":"GoTerm","value":"P:glucose catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043937","properties":[{"key":"GoTerm","value":"P:regulation of sporulation"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10388626"}]},{"database":"CDD","id":"cd16010","properties":[{"key":"EntryName","value":"iPGM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1450.10:FF:000001","properties":[{"key":"EntryName","value":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.720.10:FF:000001","properties":[{"key":"EntryName","value":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.720.10","properties":[{"key":"EntryName","value":"Alkaline Phosphatase, subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1450.10","properties":[{"key":"EntryName","value":"BPG-independent phosphoglycerate mutase, domain B"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01038","properties":[{"key":"EntryName","value":"GpmI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017850","properties":[{"key":"EntryName","value":"Alkaline_phosphatase_core_sf"}]},{"database":"InterPro","id":"IPR011258","properties":[{"key":"EntryName","value":"BPG-indep_PGM_core"}]},{"database":"InterPro","id":"IPR006124","properties":[{"key":"EntryName","value":"Metalloenzyme"}]},{"database":"InterPro","id":"IPR036646","properties":[{"key":"EntryName","value":"PGAM_B_sf"}]},{"database":"InterPro","id":"IPR005995","properties":[{"key":"EntryName","value":"Pgm_bpd_ind"}]},{"database":"NCBIfam","id":"TIGR01307","properties":[{"key":"EntryName","value":"pgm_bpd_ind"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31637","properties":[{"key":"EntryName","value":"2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31637:SF0","properties":[{"key":"EntryName","value":"2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06415","properties":[{"key":"EntryName","value":"iPGM_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01676","properties":[{"key":"EntryName","value":"Metalloenzyme"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001492","properties":[{"key":"EntryName","value":"IPGAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64158","properties":[{"key":"EntryName","value":"2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53649","properties":[{"key":"EntryName","value":"Alkaline phosphatase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKKPVALIILDGFALRDETYGNAVAQANKPNFDRYWNEYPHTTLKACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRINIAIREGEFDRNETFLAAMNHVKQHGTSLHLFGLLSDGGVHSHIHHLYALLRLAAKEGVKRVYIHGFLDGRDVGPQTAPQYIKELQEKIKEYGVGEIATLSGRYYSMDRDKRWDRVEKAYRAMVYGEGPTYRDPLECIEDSYKHGIYDEFVLPSVIVREDGRPVATIQDNDAIIFYNFRPDRAIQISNTFTNEDFREFDRGPKHPKHLFFVCLTHFSETVKGYVAFKPTNLDNTIGEVLSQHGLRQLRIAETEKYPHVTFFMSGGREEKFPGEDRILINSPKVPTYDLKPEMSAYEVTDALLKEIEADKYDAIILNYANPDMVGHSGKLEPTIKAVEAVDECLGKVVDAILAKGGIAIITADHGNADEVLTPDGKPQTAHTTNPVPVIVTKKGIKLRDGGILGDLAPTMLDLLGLPQPKEMTGKSLIVK","length":511,"molWeight":57003,"crc64":"45E4F5CEE457A04B","md5":"1BA2FD2EB32A5580B8F5C754DEDC7337"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"MASS SPECTROMETRY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":13,"Modified residue":1,"Mutagenesis":11,"Beta strand":20,"Helix":25,"Turn":4},"uniParcId":"UPI000016E39E"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"S0F332","uniProtkbId":"PAP_GEOSE","entryAudit":{"firstPublicDate":"2014-07-09","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-09-18","entryVersion":45,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Protein-arginine-phosphatase"},"shortNames":[{"value":"PAP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"}],"value":"3.9.1.2"}]},"alternativeNames":[{"fullName":{"value":"Phosphoarginine phosphatase"}}]},"genes":[{"geneName":{"value":"ywle"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"}],"value":"Catalyzes the specific dephosphorylation of phosphoarginine residues in proteins. Probably counteracts the protein arginine kinase McsB in vivo. Exhibits almost no activity against pTyr peptides. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(omega)-phospho-L-arginyl-[protein] + H2O = L-arginyl-[protein] + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43380"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:10533"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83226"}],"ecNumber":"3.9.1.2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"}],"value":"Irreversibly inhibited by the synthetic inhibitor cyc-SeCN-amidine, which inactivates the enzyme by inducing disulfide bond formation between the two active site cysteine residues Cys-9 and Cys-14"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":100.0,"unit":"mM","substrate":"p-nitrophenyl-phosphate (at 25 degrees Celsius and pH 7.6)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"}]},{"constant":124.52,"unit":"mM","substrate":"p-nitrophenyl-phosphate (at 40 degrees Celsius and pH 8.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"}],"value":"kcat is 1.12 sec(-1) with pNPP as substrate (at 25 degrees Celsius and pH 7.6) (PubMed:23838530) and 3.2 sec(-1) with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242). pNPP is a phosphotyrosine mimicking compound."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24825175"}],"value":"Is present in solution as a mixture of monomers, dimers and higher order oligomers (trimers and tetramers)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24825175"}],"value":"An engineered YwlE Ala-9 mutant can be used as a phosphatase trap that efficiently captures arginine-phosphorylated proteins but cannot hydrolyze the captured substrates, thus facilitating identification of phosphoarginine sites in the large pool of cellular protein modifications. Therefore, this novel tool for the selective enrichment and subsequent MS analysis of arginine phosphorylation should facilitate the investigation of this highly overlooked protein modification, in particular in eukaryotic samples"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the low molecular weight phosphotyrosine protein phosphatase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Protein-arginine-phosphatase","featureId":"PRO_0000429921"},{"type":"Active site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"}]},{"type":"Active site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P11064"}]},{"type":"Active site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P11064"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Important for substrate discrimination"},{"type":"Mutagenesis","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Mutant stably binds to the arginine-phosphorylated substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24825175"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Complete loss of phosphatase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24825175"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Strongly decreases p-Arg phosphatase activity and markedly increases p-Tyr phosphatase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23770242"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["I"]}},{"type":"Mutagenesis","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"6-fold reduction in phosphatase activity with pNPP as substrate. Nearly no effect on substrate affinity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23838530"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Mutant does not bind to the arginine-phosphorylated substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24825175"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A","N"]}},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Beta strand","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Beta strand","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Beta strand","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]},{"type":"Helix","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4PIC"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0904","category":"Molecular function","name":"Protein phosphatase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-92LUQ55TKHFEH","citationType":"submission","authors":["Fuhrmann Jakob J.F.","Clausen Tim T.C."],"title":"Characterization of the arginine phosphatase YwlE from Geobacillus stearothermophilus.","publicationDate":"JUN-2013","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"23838530","citationType":"journal article","authors":["Fuhrmann J.","Subramanian V.","Thompson P.R."],"citationCrossReferences":[{"database":"PubMed","id":"23838530"},{"database":"DOI","id":"10.1021/cb4001469"}],"title":"Targeting the arginine phosphatase YwlE with a catalytic redox-based inhibitor.","publicationDate":"2013","journal":"ACS Chem. Biol.","firstPage":"2024","lastPage":"2032","volume":"8"},"referencePositions":["KINETIC PARAMETERS","ACTIVITY REGULATION","ACTIVE SITE","MUTAGENESIS OF CYS-9 AND CYS-14"]},{"referenceNumber":3,"citation":{"id":"23770242","citationType":"journal article","authors":["Fuhrmann J.","Mierzwa B.","Trentini D.B.","Spiess S.","Lehner A.","Charpentier E.","Clausen T."],"citationCrossReferences":[{"database":"PubMed","id":"23770242"},{"database":"DOI","id":"10.1016/j.celrep.2013.05.023"}],"title":"Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria.","publicationDate":"2013","journal":"Cell Rep.","firstPage":"1832","lastPage":"1839","volume":"3"},"referencePositions":["FUNCTION AS AN ARGININE PHOSPHATASE","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","KINETIC PARAMETERS","MUTAGENESIS OF THR-13"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"24825175","citationType":"journal article","authors":["Trentini D.B.","Fuhrmann J.","Mechtler K.","Clausen T."],"citationCrossReferences":[{"database":"PubMed","id":"24825175"},{"database":"DOI","id":"10.1074/mcp.o113.035790"}],"title":"Chasing phosphoarginine proteins: development of a selective enrichment method using a phosphatase trap.","publicationDate":"2014","journal":"Mol. Cell. Proteomics","firstPage":"1953","lastPage":"1964","volume":"13"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PHOSPHATE","BIOTECHNOLOGY","SUBUNIT","MUTAGENESIS OF CYS-9 AND ASP-117"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HG316025","properties":[{"key":"ProteinId","value":"CDF77252.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_033017317.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CBCSGJ010000034.1"}]},{"database":"PDB","id":"4PIC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A/B=1-148"}]},{"database":"AlphaFoldDB","id":"S0F332","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"S0F332","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"89613447","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:CDF77252","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.9.1.2","properties":[{"key":"OrganismId","value":"623"}]},{"database":"EvolutionaryTrace","id":"S0F332","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0098627","properties":[{"key":"GoTerm","value":"F:protein arginine phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004725","properties":[{"key":"GoTerm","value":"F:protein tyrosine phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16344","properties":[{"key":"EntryName","value":"LMWPAP"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050438","properties":[{"key":"EntryName","value":"LMW_PTPase"}]},{"database":"InterPro","id":"IPR023485","properties":[{"key":"EntryName","value":"Ptyr_pPase"}]},{"database":"InterPro","id":"IPR036196","properties":[{"key":"EntryName","value":"Ptyr_pPase_sf"}]},{"database":"InterPro","id":"IPR017867","properties":[{"key":"EntryName","value":"Tyr_phospatase_low_mol_wt"}]},{"database":"PANTHER","id":"PTHR11717","properties":[{"key":"EntryName","value":"LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11717:SF31","properties":[{"key":"EntryName","value":"LOW MOLECULAR WEIGHT PROTEIN-TYROSINE-PHOSPHATASE ETP-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01451","properties":[{"key":"EntryName","value":"LMWPc"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00719","properties":[{"key":"EntryName","value":"LMWPTPASE"}]},{"database":"SMART","id":"SM00226","properties":[{"key":"EntryName","value":"LMWPc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52788","properties":[{"key":"EntryName","value":"Phosphotyrosine protein phosphatases I"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPYRILFVCTGNTCRSPMAAALLENKQLPGVEVKSAGVFAAEGSEASVHAKMVLKEKGIEAAHRSSQLKKEHIDWATHVLAMTSGHKDMIVERFPEAKDKTFTLKQFVSGTDGDIADPFGGPIEVYRAARDELETLIDRLAEKLQTEQ","length":148,"molWeight":16300,"crc64":"7C321C8E3F888D14","md5":"E736CD4714B0081614059FA873B0F881"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"BIOTECHNOLOGY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":3,"Binding site":1,"Site":1,"Mutagenesis":5,"Beta strand":4,"Helix":8},"uniParcId":"UPI00035155FD"}}]}