{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TXJ1","uniProtkbId":"A0A497TXJ1_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20478.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"4.2.1.59"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"Beta-hydroxyacyl-ACP dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"(3R)-hydroxymyristoyl-ACP dehydrase"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"UDP-3-O-acyl-N-acetylglucosamine deacetylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"UDP-3-O-acyl-GlcNAc deacetylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"3.5.1.108"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"lpxC"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"fabZ"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20478.1"}],"value":"B0G92_2621"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002923"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13097"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"4.2.1.59","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67816"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:137740"},{"database":"ChEBI","id":"CHEBI:173225"}],"ecNumber":"3.5.1.108","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024535"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"Belongs to the LpxC family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"value":"Belongs to the thioester dehydratase family. FabZ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061355"}],"value":"In the C-terminal section; belongs to the thioester dehydratase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061221"}],"value":"In the N-terminal section; belongs to the LpxC family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20478.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}]},{"type":"Active site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}]},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022556"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"id":"KW-0441","category":"Biological process","name":"Lipid A biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20478.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20478.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000009","properties":[{"key":"ProteinId","value":"PKW20478.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056073741.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALHAS010000010.1"}]},{"database":"AlphaFoldDB","id":"A0A497TXJ1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019171","properties":[{"key":"GoTerm","value":"F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0103117","properties":[{"key":"GoTerm","value":"F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01288","properties":[{"key":"EntryName","value":"FabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000001","properties":[{"key":"EntryName","value":"3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.20","properties":[{"key":"EntryName","value":"lpxc deacetylase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1700.10","properties":[{"key":"EntryName","value":"lpxc deacetylase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00406","properties":[{"key":"EntryName","value":"FabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00388","properties":[{"key":"EntryName","value":"LpxC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013114","properties":[{"key":"EntryName","value":"FabA_FabZ"}]},{"database":"InterPro","id":"IPR010084","properties":[{"key":"EntryName","value":"FabZ"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR004463","properties":[{"key":"EntryName","value":"UDP-acyl_GlcNac_deAcase"}]},{"database":"InterPro","id":"IPR011334","properties":[{"key":"EntryName","value":"UDP-acyl_GlcNac_deAcase_C"}]},{"database":"InterPro","id":"IPR015870","properties":[{"key":"EntryName","value":"UDP-acyl_N-AcGlcN_deAcase_N"}]},{"database":"NCBIfam","id":"NF000582","properties":[{"key":"EntryName","value":"fabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01750","properties":[{"key":"EntryName","value":"fabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00325","properties":[{"key":"EntryName","value":"lpxC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009667","properties":[{"key":"EntryName","value":"PRK13188.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33694","properties":[{"key":"EntryName","value":"UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33694:SF1","properties":[{"key":"EntryName","value":"UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07977","properties":[{"key":"EntryName","value":"FabA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03331","properties":[{"key":"EntryName","value":"LpxC"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVKQKTIKNEISLTGVGLHTGKEVKMTFKPAPINNGFTFVRVDLEGQPIIEADANYVVNTQRGTNLEKKGVKIQTSEHVLAAFIGCDIDNVIIELDASEPPIMDGSSKFFVEAIEKAGIEEQDAERKVYVVKEVISYTDEATGSEILVMPSDDYQVTTMVDFGTKVLGTQNATMKSIADFKTEIADARTFSFLHELEALLENGLIKGGDLNNAIVYVDKEISDSTMENLKVAFGKDKISVKPNGVLDNLTLHYPNEAARHKLLDVVGDLALIGMKIKGKVIANKPGHFVNTQFAKKMSKIIKIEQRNQVPVYDLNQEPLMDIHKIMSILPHRPPFLFIDRIIEMSDTHVVGLKNVTMNESFFVGHFPGAPVMPGVIIVEAMAQTGGILILSSVPDPENYLTYFMKIDNVKFKQKVLPGDSLIFKCDLMSPIRRGICQMQASAYANGRLVAEAELMAQISKTN","length":462,"molWeight":51078,"crc64":"B00B95877E3C2769","md5":"ED6B03E4071450EB652D7AC7571512B2"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Active site":2,"Binding site":3},"uniParcId":"UPI0007019335"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U5Z6","uniProtkbId":"A0A497U5Z6_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29975.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29975.1"}],"value":"B0G92_1623"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29975.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":512,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29975.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29975.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW29975.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101471720.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497U5Z6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","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":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"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":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNQTKYIFVTGGVTSSLGKGIIAASLAKLLQARGYRTTIQKFDPYINVDPGTLNPYEHGECYVTDDGAETDLDLGHYERFLNVPTSQANNVTTGRVYLSVIEKERRGEFLGKTVQVVPHITNEIKERMQLLGKTGEFDIVITEIGGTVGDIESLPYIESVRQLVWELGENNGIVIHLTLVPYLAAAGELKTKPTQHSVKALMESGIKADILVCRTEHELSDELRQKLALFCNVKREAVIQSIDASTIYDVPNLMLEEGLDKVALKKLDLPEKATPDLKQWNEFLQKLKNPKHIVNIGLVGKYVELQDSYKSILEAFIHAGAANETKVNVVSIHSEYVDEKNIADKLRDLDGILVAPGFGERGIEGKIDTVRYARENNIPFFGICLGMQMAVIEYSRNVLGYSDANSTEMNAGTAHPVINLMEEQKTITDKGGTMRLGAWKCEIKPDTLASKIYGKNQIQERHRHRYEFNGEYLEELENAGLKASGINPDTNLVEIIEIEKHPFFIGVQYHPEYKSTVAQPHPLFVSFVKAAVTHKNK","length":537,"molWeight":59985,"crc64":"2BB2CF403913D55B","md5":"6A5255E432DFB14D66E602BFBD79642F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":17},"uniParcId":"UPI000C70045D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U8R1","uniProtkbId":"A0A497U8R1_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20643.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20643.1"}],"value":"B0G92_2793"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"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:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","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:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20643.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20643.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20643.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000009","properties":[{"key":"ProteinId","value":"PKW20643.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056073362.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALHAS010000011.1"}]},{"database":"AlphaFoldDB","id":"A0A497U8R1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"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:UniProtKB-UniRule"}]},{"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:UniProtKB-UniRule"}]},{"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":"MSKTIKKIGVLTSGGDSPGMNAAIRSVVRTCAYHNIECIGIYRGYQGMIEGDFKEMGPRSVNNIINKGGTILKSARSKEFMTEEGRKKAHSNLSAAGVEALVVIGGDGSFTGGLVFNKEYGFPIIGIPGTIDNDIFGTTHTLGYDTALNTVVEAIDKIRDTASSHNRLFFVEVMGRDAGHIALNAGIGAGAEEILIPEEDLGLDRLLESLRKSKLSGKSSSIVVIAEGDKIGKNVFELKDYVEENMPEYDVRVSVLGHMQRGGAPSCFDRVLASRLGVKAVESILDGKSNYMVGLLNDKIELTPLEQAIKGHSQIDRELLRVSDIMTT","length":328,"molWeight":35351,"crc64":"09E7417CBAA467F8","md5":"94F38BA7D1061B0B5B733F55D8284592"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":14},"uniParcId":"UPI0006F86DB1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497UHT4","uniProtkbId":"A0A497UHT4_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ftsH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"}],"value":"B0G92_2555"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010550"}],"value":"In the N-terminal section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Transmembrane","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Coiled coil","location":{"start":{"value":592,"modifier":"EXACT"},"end":{"value":619,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Active site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21270.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000008","properties":[{"key":"ProteinId","value":"PKW21270.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472447.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000008.1"}]},{"database":"AlphaFoldDB","id":"A0A497UHT4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000019","properties":[{"key":"EntryName","value":"AFG3-like AAA ATPase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000003","properties":[{"key":"EntryName","value":"AFG3-like AAA ATPase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1690.20","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":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR050928","properties":[{"key":"EntryName","value":"ATP-dep_Zn_Metalloprotease"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43655:SF2","properties":[{"key":"EntryName","value":"AFG3 LIKE MATRIX AAA PEPTIDASE SUBUNIT 2, ISOFORM A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43655","properties":[{"key":"EntryName","value":"ATP-DEPENDENT PROTEASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"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":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKDNNTNPNPKKFRLSPWWIYGGLILFFFILNWASGGSSWGETSKASASDFNKLLEKGQIEKVVVYNKNEAEIFLNKEGLADPANKKVTKDIFDKPNPGPHYILDNIGNDELFQKKLETAQQEGKLKDYNFLPKSNWSEIFIALLPILIIVGIWLFIMRRMSGGGAAGGGGQIFNIGKSKAKLFDEKTDVKVTFKDVAGLEGAKEEVQEIVEFLKSPEKYTNLGGKIPKGALLVGPPGTGKTLLAKAVAGEAKVPFFSLSGSDFVEMFVGVGASRVRDLFKQAKEKSPAIIFIDEIDAVGRARGKNNISGSNDERENTLNQLLTEMDGFGTNTNVIVLAATNRADVLDKALMRAGRFDRQIYVDLPDIRERKEIFEVHLGPLKKVEGLDTDFLAKQTPGFSGADIANVCNEAALIAARKDKKAVDKQDFLDAVDRIIGGLEKKNKIITPEEKRAIAIHEAGHATVSWMLEHAAPLIKVTIVPRGQSLGAAWYLPEERQIVRTDQMLDEMCATMGGRAAEKVTFNRISTGALSDLEKVTKQARAMITVYGLNDKLGNVTYYDSSGQSEYNFSKPYSEDTAKIIDKEISDLIEGQYQRAIKILEENKDKLNQLADILIEKEVIFKDDLETIFGKRAFGEAVEEVFEE","length":646,"molWeight":71533,"crc64":"D687E06F606BC994","md5":"212E14BB0B72A4DDDF64BC0BBDF6A739"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Transmembrane":2,"Domain":1,"Coiled coil":1,"Active site":1,"Binding site":4},"uniParcId":"UPI000C70E1EE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497UK75","uniProtkbId":"A0A497UK75_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21024.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21024.1"}],"value":"B0G92_2304"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21024.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21024.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW21024.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000008","properties":[{"key":"ProteinId","value":"PKW21024.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472279.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000008.1"}]},{"database":"AlphaFoldDB","id":"A0A497UK75","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVLSGKKIVLGVSGGIAAYKTASLVRLFIKAGADVQVVMTPASKDFVTPLTLSTLSKNPVHSTFYNDDEEAVWNNHVELGLWADLMLVAPATANTLSKMANGSCDNLLIATYLSAKCPVYFAPAMDLDMYKHPSTLASFKLLRQFGNIMIPAESGELASGLSGEGRMAEPENIIAFLEADLESKLPLKGKKILVTAGPTYEAIDPVRFIGNHSSGKMGFDIAEHAAGLGAEVILISGPTHLKPKSSGITLVNVTSAQEMYEAAHRYFGDVDVAISAAAVADYRPKFPATQKIKKTEDAFTIELEKTQDILASLGKVKQKQFLIGFALETENEIENAKLKIQKKNLDLIVLNSLQDEGAGFGKPTNKITFIDRNLEIEPMPLKTKEAVAEDILNKVIQHFYA","length":402,"molWeight":43531,"crc64":"B1D890974C327B67","md5":"79E88733842EE2D0BBC7590AC768A065"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":5},"uniParcId":"UPI000C70E8DE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497UVP4","uniProtkbId":"A0A497UVP4_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29449.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29449.1"}],"value":"B0G92_1085"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29449.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29449.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29449.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29449.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW29449.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_180326401.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497UVP4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIILKDILYKVAIEAVKGSTEIAINAINFDSRKIENNDVFIAIRGTVADGHEYIETAISKGAIAIICDTFPENIVSGVTYVQVKDTNRALAFIASNYYGNPSANLKLVGITGTNGKTTIASLLYQLFKKAGYKVGLLSTVKNVVDDVEYKSMLTTSDSITINKFLKEMNDVGVEYCFMEVSSHGIAQKRTEGLQFAGGVFTNLSHDHLDYHKTFAEYRDVKKTFFDQLPKGAFALVNIDDKNGPVMLQNTNAKKLTYALKSYADYRAQILENQLSGLLLKINEQEVWVRLIGNFNAYNLLAIYGTAVELGLDTMEVLRLLSELESVSGRFQYIVSKGNITAVVDYAHTPDALENVLKTIDDIRTKNEQLITIVGCGGDRDKTKRPIMANIASTLSDKAILTSDNPRTEDPEAIILEMEKGVEPQNYKKTLAIVDRKQAIKTACQLAQPKDIILIAGKGHETYQEINGVRYDFDDMKIVTELLEQLNK","length":487,"molWeight":54101,"crc64":"5C6210ADA5271144","md5":"CE5F17B314108ADC611D902402D52F07"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI000CC81915"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497UVR4","uniProtkbId":"A0A497UVR4_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29430.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29430.1"}],"value":"B0G92_1066"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29430.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29430.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29430.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW29430.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101471330.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497UVR4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"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:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"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_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQIEKKDIRALSKDQLREFFVSNGDKAFRGNQVYEWLWNKGAHNFDDMTNVAKATRQMLEENFVINHIRVDQMQKSEDGTVKNAVRLHDGLVVESVLIPTETRTTACVSSQVGCSLDCNFCATARLKRMRNLNPDEIYDQVVAIDNESRLYHNRPLSNIVFMGMGEPLMNYNNVMKAIEKIVSPEGLGMSPKRITVSTSGVPKMIKKLADDEVKFKLAVSLHSAIDEIRSQIMPFSKSFPLADLREALEYWYSHTKSRVTYEYVVWKGINDNKASVDALVKFCKYVPCKVNLIEYNPIDDGEFQQASEESINEYIKALERNDIVVKVRRSRGKDIDAACGQLANKEA","length":347,"molWeight":39518,"crc64":"ED67D760ED79AB03","md5":"5535CB4C4C4C6E96CF79FD89B8F9ABD3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI000C71599E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497UZQ8","uniProtkbId":"A0A497UZQ8_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29091.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"2-amino-3-ketobutyrate coenzyme A ligase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"AKB ligase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"2.3.1.29"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Glycine acetyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"kbl"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29091.1"}],"value":"B0G92_0720"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055827"}],"value":"Involved in de novo bacterial ceramide synthesis. Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine. Also capable of using alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa). Contributes to the levels of endogenous sphingolipids in its host"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-serine + hexadecanoyl-CoA + H(+) = 3-oxosphinganine + CO2 + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14761"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:58299"}],"ecNumber":"2.3.1.50","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047854"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:14762"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047854"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycine + acetyl-CoA = (2S)-2-amino-3-oxobutanoate + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20736"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:78948"}],"ecNumber":"2.3.1.29","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Binds 1 pyridoxal phosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004746"}],"value":"Cofactor biosynthesis; biotin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004760"}],"value":"Lipid metabolism; sphingolipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004991"}],"value":"Sphingolipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010008"}],"value":"Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29091.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"Aminotransferase class I/classII large","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00155"}]},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29091.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022919"}],"id":"KW-0746","category":"Biological process","name":"Sphingolipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29091.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29091.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW29091.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056067603.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALHAS010000013.1"}]},{"database":"AlphaFoldDB","id":"A0A497UZQ8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008890","properties":[{"key":"GoTerm","value":"F:glycine C-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004758","properties":[{"key":"GoTerm","value":"F:serine C-palmitoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006567","properties":[{"key":"GoTerm","value":"P:L-threonine catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030148","properties":[{"key":"GoTerm","value":"P:sphingolipid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd06454","properties":[{"key":"EntryName","value":"KBL_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000004","properties":[{"key":"EntryName","value":"2-amino-3-ketobutyrate coenzyme A ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000006","properties":[{"key":"EntryName","value":"5-aminolevulinate synthase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00985","properties":[{"key":"EntryName","value":"2am3keto_CoA_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011282","properties":[{"key":"EntryName","value":"2am3keto_CoA_ligase"}]},{"database":"InterPro","id":"IPR004839","properties":[{"key":"EntryName","value":"Aminotransferase_I/II_large"}]},{"database":"InterPro","id":"IPR050087","properties":[{"key":"EntryName","value":"AON_synthase_class-II"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR01822","properties":[{"key":"EntryName","value":"2am3keto_CoA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF005394","properties":[{"key":"EntryName","value":"PRK06939.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693:SF103","properties":[{"key":"EntryName","value":"AMINOTRANSFERASE CLASS I_CLASSII DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693","properties":[{"key":"EntryName","value":"CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00155","properties":[{"key":"EntryName","value":"Aminotran_1_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYGKIQQYLQEELQTIEDNGIFKKERIITSPQGAEITISTGEKVLNFCANNYLGLSSHPEVVQAAKDALDTHGFGMSSVRFICGTQDIHKTLEKKIADFYGTEDTILYAAAFDANGGVFEPLFGENDAIISDSLNHASIIDGVRLCKAARYRYENSNMEDLEQQLIKANEAGHRFKIIVTDGVFSMDGLVAPLDKICDLADKYDALVMVDECHAAGFIGATGKGTLEAKGVMGRVDIVTGTLGKALGGAMGGYTTAKKEIIELLRQRSRPYLFSNSLAPSIVGASIKVFELLEKDTTLRDKLEWNTNYFKKGMKEAGFDIIDGDSAIVPVMLYDAKLSQNMANELLKEGIYVIGFFFPVVPRDKARIRVQLSAAHTKEHLDAAIQAFTTVGKRLNVI","length":397,"molWeight":43587,"crc64":"92FF03FCF50482D8","md5":"293D0DD818C154F43552CB3EB104EBFE"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":4,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":5,"Modified residue":1},"uniParcId":"UPI0006F4B680"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TVC9","uniProtkbId":"A0A497TVC9_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20012.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"GTP cyclohydrolase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"3.5.4.16"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"GTP cyclohydrolase I"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"GTP-CH-I"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"folE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20012.1"}],"value":"B0G92_3252"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17473"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:58462"}],"ecNumber":"3.5.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"Homopolymer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008085"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"Belongs to the GTP cyclohydrolase I family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20012.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"GTP cyclohydrolase I","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01227"}]},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20012.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20012.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000012","properties":[{"key":"ProteinId","value":"PKW20012.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056072861.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALHAS010000014.1"}]},{"database":"AlphaFoldDB","id":"A0A497TVC9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003934","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase I activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006730","properties":[{"key":"GoTerm","value":"P:one-carbon metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006729","properties":[{"key":"GoTerm","value":"P:tetrahydrobiopterin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046654","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.30.1130.10:FF:000001","properties":[{"key":"EntryName","value":"GTP cyclohydrolase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.286.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1130.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00223","properties":[{"key":"EntryName","value":"FolE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043133","properties":[{"key":"EntryName","value":"GTP-CH-I_C/QueF"}]},{"database":"InterPro","id":"IPR043134","properties":[{"key":"EntryName","value":"GTP-CH-I_N"}]},{"database":"InterPro","id":"IPR001474","properties":[{"key":"EntryName","value":"GTP_CycHdrlase_I"}]},{"database":"InterPro","id":"IPR018234","properties":[{"key":"EntryName","value":"GTP_CycHdrlase_I_CS"}]},{"database":"InterPro","id":"IPR020602","properties":[{"key":"EntryName","value":"GTP_CycHdrlase_I_dom"}]},{"database":"NCBIfam","id":"NF006824","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006825","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006826","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00063","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11109:SF7","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11109","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01227","properties":[{"key":"EntryName","value":"GTP_cyclohydroI"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55620","properties":[{"key":"EntryName","value":"Tetrahydrobiopterin biosynthesis enzymes-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00859","properties":[{"key":"EntryName","value":"GTP_CYCLOHYDROL_1_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00860","properties":[{"key":"EntryName","value":"GTP_CYCLOHYDROL_1_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNNEDFLDEIGDNHIATNAKNPLRSDAFDITDDQKIELIKKDVENILLTLGMDLTDDSLKGTPNRVAKMFVKEIFGGLNPAKKPNASTFINNYKYGEMLVEKNITVYSTCEHHLLPIIGRAHVAYISNGKVVGLSKMNRIVEYFAKRPQVQERLTMQIVQELQKVLNTEDVACVIDAKHLCVNSRGIKDIESSTVTSEFGGKFKNEATRREFLDYIKFDTQF","length":223,"molWeight":25279,"crc64":"BFE19AD0EA3BEB8F","md5":"12CF9341B2EE2FFF526146AF6ADE0ADA"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3},"uniParcId":"UPI0006FA9D88"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TWS6","uniProtkbId":"A0A497TWS6_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20392.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003331"}],"value":"Adenylate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"AK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003331"}],"value":"2.7.4.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"ATP-AMP transphosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"ATP:AMP phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"Adenylate monophosphate kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"adk"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20392.1"}],"value":"B0G92_3104"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AMP + ATP = 2 ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12973"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003331"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003331"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003331"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and disassembling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003330"}],"value":"Belongs to the adenylate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20392.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"NMP","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003331"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022727"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"id":"KW-0545","category":"Biological process","name":"Nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00235"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20392.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20392.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000010","properties":[{"key":"ProteinId","value":"PKW20392.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056068895.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALHAS010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A497TWS6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004017","properties":[{"key":"GoTerm","value":"F:AMP kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044209","properties":[{"key":"GoTerm","value":"P:AMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01428","properties":[{"key":"EntryName","value":"ADK"},{"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":"HAMAP","id":"MF_00235","properties":[{"key":"EntryName","value":"Adenylate_kinase_Adk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000850","properties":[{"key":"EntryName","value":"Adenylat/UMP-CMP_kin"}]},{"database":"InterPro","id":"IPR033690","properties":[{"key":"EntryName","value":"Adenylat_kinase_CS"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF001381","properties":[{"key":"EntryName","value":"PRK00279.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011100","properties":[{"key":"EntryName","value":"PRK14527.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011101","properties":[{"key":"EntryName","value":"PRK14528.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011104","properties":[{"key":"EntryName","value":"PRK14531.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011105","properties":[{"key":"EntryName","value":"PRK14532.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23359","properties":[{"key":"EntryName","value":"NUCLEOTIDE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00406","properties":[{"key":"EntryName","value":"ADK"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00094","properties":[{"key":"EntryName","value":"ADENYLTKNASE"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00113","properties":[{"key":"EntryName","value":"ADENYLATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MINIVLFGKPGAGKGTQAEFLKKKYNLTHLSTGDIFRFNIKNETELGKLAKTYMDKGDLVPDEVTIQMLQSEVDKNPESKGFLFDGFPRTLSQAKALDNFLESKNEEITATVALEANDEILVKRLLERGKTSGRPDDQDEEKIRNRYQEYNEKTAPLMDYYKAQNKFHAVDGIGSIEEITHRLSTVIDSL","length":190,"molWeight":21535,"crc64":"FD603ACD177A1073","md5":"A800615B33475367F5E7D2293238D5ED"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Region":1,"Binding site":10},"uniParcId":"UPI0006FFD5A0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TWY9","uniProtkbId":"A0A497TWY9_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20332.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthase small chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthetase glutamine chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"carA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20332.1"}],"value":"B0G92_3044"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049285"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007800"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20332.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Carbamoyl-phosphate synthase small subunit N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01097"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"CPSase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]},{"type":"Active site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20332.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20332.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000010","properties":[{"key":"ProteinId","value":"PKW20332.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472846.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000010.1"}]},{"database":"AlphaFoldDB","id":"A0A497TWY9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050472","properties":[{"key":"EntryName","value":"Anth_synth/Amidotransfase"}]},{"database":"InterPro","id":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418:SF7","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418","properties":[{"key":"EntryName","value":"MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00097","properties":[{"key":"EntryName","value":"ANTSNTHASEII"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKYTTRQKAILLLSDGTIFYGKSIGIEGTTFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNEEDVESDQIMISGLVCKNFSFNYSRANSSGSLEDYFKKQNLICISDVDTRALVSYIRDNGAMNAVISTDGKSIEELKEMLAKVPNMEGLELASKVSTKAPYFVGEETATYRIAALDLGIKKNILRNLAKRDCYIKVFPFDTTYEEMKAFNPDGFFLSNGPGDPDPLFGAIEIAKKILSNDDPVFGICLGHQVLALANGIPTYKMFNGHRGINHPVMNVITGKGEITSQNHGFAVNREALEKHPDLEITHLHINDGTVAGMRMKNKNCFSVQYHPEASPGPHDSSYLFDQFIEKIKSCVAK","length":370,"molWeight":40919,"crc64":"7FE70F0858E2625A","md5":"E58F88718BAE38F5B78E3D86C96F5C65"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Active site":3,"Binding site":8},"uniParcId":"UPI000C70C37B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TXK8","uniProtkbId":"A0A497TXK8_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20498.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Endonuclease V"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"3.1.21.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Deoxyinosine 3'endonuclease"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Deoxyribonuclease V"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"DNase V"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"nfi"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20498.1"}],"value":"B0G92_2641"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.","ecNumber":"3.1.21.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Belongs to the endonuclease V family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20498.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Interaction with target DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20498.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20498.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000009","properties":[{"key":"ProteinId","value":"PKW20498.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_180326444.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBCNKL010000006.1"}]},{"database":"AlphaFoldDB","id":"A0A497TXK8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043737","properties":[{"key":"GoTerm","value":"F:deoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016891","properties":[{"key":"GoTerm","value":"F:RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003727","properties":[{"key":"GoTerm","value":"F:single-stranded RNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06559","properties":[{"key":"EntryName","value":"Endonuclease_V"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.2170.10","properties":[{"key":"EntryName","value":"archaeoglobus fulgidus dsm 4304 superfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00801","properties":[{"key":"EntryName","value":"Endonuclease_5"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR007581","properties":[{"key":"EntryName","value":"Endonuclease-V"}]},{"database":"PANTHER","id":"PTHR28511","properties":[{"key":"EntryName","value":"ENDONUCLEASE V"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR28511:SF1","properties":[{"key":"EntryName","value":"ENDONUCLEASE V"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04493","properties":[{"key":"EntryName","value":"Endonuclease_5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLNYDNFTIEMATRLQNEMKENISLKTRNKNISTIAGADISHEVGSSKLYAGIVILSYPDLIPLSYSLAVGESKFEYKAEYLAFREVPTLIKAWEQIPVKPDLLILDGQGITHPRRMGIASHFGLLTDHPTIGCAKNMLHGKYDVLEDEKFSFRPIYKNQDKLGFALRTKTHVKPVFISPGHHMSVDDSLEIMNRTVQKYRIPEPTRQAHVMVNLFRTGQRQAGYHEFDVQLPLF","length":235,"molWeight":26834,"crc64":"07005CBECAF5E0FB","md5":"AF32DBCE9041DE377463F0F2932BB366"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":2,"Site":1},"uniParcId":"UPI000CC36BEC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TYM9","uniProtkbId":"A0A497TYM9_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW19978.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019357"}],"value":"Dihydrofolate synthase/folylpolyglutamate synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013023"}],"value":"6.3.2.12"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013025"}],"value":"6.3.2.17"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032510"}],"value":"Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030048"}],"value":"Folylpolyglutamate synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030592"}],"value":"Tetrahydrofolylpolyglutamate synthase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW19978.1"}],"value":"B0G92_3326"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002714"}],"value":"Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51912"},{"database":"Rhea","id":"RHEA-COMP:13257"},{"database":"Rhea","id":"RHEA-COMP:13258"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:136572"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049035"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10580"},{"database":"Rhea","id":"RHEA-COMP:14738"},{"database":"Rhea","id":"RHEA-COMP:14740"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:141005"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047493"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51904"},{"database":"Rhea","id":"RHEA-COMP:13088"},{"database":"Rhea","id":"RHEA-COMP:14300"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:134413"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047808"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7,8-dihydropteroate + L-glutamate + ATP = 7,8-dihydrofolate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23584"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17839"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57451"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049161"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004799"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005150"}],"value":"Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008276"}],"value":"Belongs to the folylpolyglutamate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW19978.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022909"}],"id":"KW-0289","category":"Biological process","name":"Folate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW19978.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW19978.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000013","properties":[{"key":"ProteinId","value":"PKW19978.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101473042.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A497TYM9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"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:0008841","properties":[{"key":"GoTerm","value":"F:dihydrofolate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004326","properties":[{"key":"GoTerm","value":"F:tetrahydrofolylpolyglutamate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"3.40.1190.10:FF:000011","properties":[{"key":"EntryName","value":"Folylpolyglutamate synthase/dihydrofolate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001645","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth"}]},{"database":"InterPro","id":"IPR018109","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth_CS"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"NCBIfam","id":"TIGR01499","properties":[{"key":"EntryName","value":"folC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11136:SF0","properties":[{"key":"EntryName","value":"DIHYDROFOLATE SYNTHETASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11136","properties":[{"key":"EntryName","value":"FOLYLPOLYGLUTAMATE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001563","properties":[{"key":"EntryName","value":"Folylpolyglu_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01011","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01012","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTYTETLDWMFSQLPMYQKQGASAYKEDLTNTVLLANHLHHPEKNIKTIHVAGTNGKGSTSHFLASILQEAGYKTGLYTSPHLKDFRERIKIDGKEISEDFVIQFIAANKSFFEQNQLSFFEMTVGLAFDYFRQEKVDIAIIEVGMGGRLDSTNIISPLLSVITNIGMDHVQFLGNTMEKIAFEKAGIIKPKTPVVIGEYTTETRPVFEKRATEMQSEIYFASDLTNTTFPSTLTGDYQEQNKKTVLQAVRALQSQGNFLISEENIKDGLWNVIKNTGLQGRWQQLKEAPKVICDTAHNKHGLEIVMKQVARQKFDILHIVLGVVNDKDLDDVLPLFPKNAKYYFCRPNIPRGLDATALQEKAATFGLNGKVYSSVAEAYKNALENASETDFIYIGGSTFVVAEIL","length":406,"molWeight":45588,"crc64":"F2397890172F2FA4","md5":"229E37790C593F5C7B4EC1567ED21C38"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI000C70E3F2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TYQ4","uniProtkbId":"A0A497TYQ4_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":26,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29991.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Succinate--CoA ligase [ADP-forming] subunit beta"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"6.2.1.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Succinyl-CoA synthetase subunit beta"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"SCS-beta"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"sucC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29991.1"}],"value":"B0G92_1640"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + succinate + CoA = succinyl-CoA + GDP + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22120"},{"database":"ChEBI","id":"CHEBI:30031"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57292"},{"database":"ChEBI","id":"CHEBI:58189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"succinate + ATP + CoA = succinyl-CoA + ADP + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17661"},{"database":"ChEBI","id":"CHEBI:30031"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57292"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.2.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Heterotetramer of two alpha and two beta subunits"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009182"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Belongs to the succinate/malate CoA ligase beta subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29991.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"substrate","note":"ligand shared with subunit alpha"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"ligand":{"name":"substrate","note":"ligand shared with subunit alpha"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022532"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00558"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29991.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29991.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW29991.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056070435.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEUTX010000026.1"}]},{"database":"AlphaFoldDB","id":"A0A497TYQ4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042709","properties":[{"key":"GoTerm","value":"C:succinate-CoA ligase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004775","properties":[{"key":"GoTerm","value":"F:succinate-CoA ligase (ADP-forming) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006104","properties":[{"key":"GoTerm","value":"P:succinyl-CoA metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006099","properties":[{"key":"GoTerm","value":"P:tricarboxylic acid cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.30.1490.20:FF:000002","properties":[{"key":"EntryName","value":"Succinate--CoA ligase [ADP-forming] subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000002","properties":[{"key":"EntryName","value":"Succinate--CoA ligase [ADP-forming] subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.261:FF:000001","properties":[{"key":"EntryName","value":"Succinate--CoA ligase [ADP-forming] subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.261","properties":[{"key":"EntryName","value":"Succinyl-CoA synthetase domains"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00558","properties":[{"key":"EntryName","value":"Succ_CoA_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013650","properties":[{"key":"EntryName","value":"ATP-grasp_succ-CoA_synth-type"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR005811","properties":[{"key":"EntryName","value":"SUCC_ACL_C"}]},{"database":"InterPro","id":"IPR005809","properties":[{"key":"EntryName","value":"Succ_CoA_ligase-like_bsu"}]},{"database":"InterPro","id":"IPR016102","properties":[{"key":"EntryName","value":"Succinyl-CoA_synth-like"}]},{"database":"NCBIfam","id":"NF001913","properties":[{"key":"EntryName","value":"sucC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01016","properties":[{"key":"EntryName","value":"sucCoAbeta"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11815:SF10","properties":[{"key":"EntryName","value":"SUCCINATE--COA LIGASE [GDP-FORMING] SUBUNIT BETA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11815","properties":[{"key":"EntryName","value":"SUCCINYL-COA SYNTHETASE BETA CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08442","properties":[{"key":"EntryName","value":"ATP-grasp_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00549","properties":[{"key":"EntryName","value":"Ligase_CoA"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001554","properties":[{"key":"EntryName","value":"SucCS_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52210","properties":[{"key":"EntryName","value":"Succinyl-CoA synthetase domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDIHEYQGKEILASYGVKVQRGYVANNPQEAVAVAKQLTAETGTGWHVIKAQVHAGGRGKGGGVKLAKNLQQVEELAEQIIGMQLITPQTSAEGKKVHKVLVAEDVYYPGESETSEFYMSVLLNRGKGRNMIMYSTEGGMDIEEVAEKTPHLIFTEEIDPTVGLQAFQARRIAFNLGLSGNAFKEMVQFVDSLYKAYVGSDASMFEINPVLKTSDNKIIAVDAKVNLDDNALYRHPALAEMRDIREENPIEVEAKAAGLNYVDLDGTVGCMVNGAGLAMATMDLIKYAGFEPANFLDVGGTADAKRVELAFRIILKDPNVKAILINIFGGIVRCDRVAQGVIDAYKNMGDSINVPIIVRLQGTNAELAKEMIDNSGMPILSAVQFQEAADQVKAALS","length":397,"molWeight":43073,"crc64":"5DCAC4B66A4955D1","md5":"5E659834D0734670F41FE58C4AB21F23"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":8},"uniParcId":"UPI0006F309E7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TZU3","uniProtkbId":"A0A497TZU3_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20082.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"Queuine tRNA-ribosyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"2.4.2.29"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"Guanine insertion enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"tRNA-guanine transglycosylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"tgt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20082.1"}],"value":"B0G92_3158"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-aminomethyl-7-carbaguanosine(34) in tRNA + guanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24104"},{"database":"Rhea","id":"RHEA-COMP:10341"},{"database":"Rhea","id":"RHEA-COMP:10342"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:58703"},{"database":"ChEBI","id":"CHEBI:74269"},{"database":"ChEBI","id":"CHEBI:82833"}],"ecNumber":"2.4.2.29","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050112"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"tRNA modification; tRNA-queuosine biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"Belongs to the queuine tRNA-ribosyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20082.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"tRNA-guanine(15) transglycosylase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01702"}]},{"type":"Region","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"RNA binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}]},{"type":"Region","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"RNA binding; important for wobble base 34 recognition","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}]},{"type":"Active site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}]},{"type":"Active site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}]},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022785"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"id":"KW-0671","category":"Biological process","name":"Queuosine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00168"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20082.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20082.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000011","properties":[{"key":"ProteinId","value":"PKW20082.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A497TZU3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008479","properties":[{"key":"GoTerm","value":"F:tRNA-guanosine(34) queuine transglycosylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008616","properties":[{"key":"GoTerm","value":"P:tRNA queuosine(34) biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.20.20.105:FF:000001","properties":[{"key":"EntryName","value":"Queuine tRNA-ribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.105","properties":[{"key":"EntryName","value":"Queuine tRNA-ribosyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00168","properties":[{"key":"EntryName","value":"Q_tRNA_Tgt"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004803","properties":[{"key":"EntryName","value":"TGT"}]},{"database":"InterPro","id":"IPR036511","properties":[{"key":"EntryName","value":"TGT-like_sf"}]},{"database":"InterPro","id":"IPR002616","properties":[{"key":"EntryName","value":"tRNA_ribo_trans-like"}]},{"database":"NCBIfam","id":"TIGR00430","properties":[{"key":"EntryName","value":"Q_tRNA_tgt"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00449","properties":[{"key":"EntryName","value":"tgt_general"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46499","properties":[{"key":"EntryName","value":"QUEUINE TRNA-RIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46499:SF1","properties":[{"key":"EntryName","value":"QUEUINE TRNA-RIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01702","properties":[{"key":"EntryName","value":"TGT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51713","properties":[{"key":"EntryName","value":"tRNA-guanine transglycosylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPKVWDKEKRMKFELLQNDPNSKARAGKITTDHGVIETPIFMPVGTVASVKGVHQRELKNDINPDIILGNTYHLYLRPQTDILEKAGGLHKFMNWDRNILTDSGGYQVYSLSSNRKIKEEGVKFKSHIDGSYHVFTPENVMEIQRTIGADIIMAFDECTPYPCDYRYAQRSMHMTHRWLDRCISHLDKVPYKYGYEQTFFPIVQGSTYKDLRQQSAEYIANAGAEGNAIGGLSVGEPAEEMYAMTEVVTEILPKDKPRYLMGVGTPINILENIALGIDMFDCVMPTRNARNGMLFTAHGTINIKNKKWESDFSPLDEMGHTFVDTEYTKAYLRHLFAANEYLGKQIATIHNLGFYMWLVREARKHILAGDFRVWKEMMVKQMDQRL","length":387,"molWeight":44479,"crc64":"C757EADE88E28D99","md5":"2A88399FBC3729BB17BADDBFD8E959D0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Active site":2,"Binding site":4},"uniParcId":"UPI000A5557A1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497TZX0","uniProtkbId":"A0A497TZX0_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20018.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"DNA gyrase subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"5.6.2.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"gyrB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20018.1"}],"value":"B0G92_3258"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent breakage, passage and rejoining of double-stranded DNA.","ecNumber":"5.6.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010708"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Belongs to the type II topoisomerase GyrB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20018.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":572,"modifier":"EXACT"}},"description":"Toprim","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50880"}]},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":539,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Site","location":{"start":{"value":484,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]},{"type":"Site","location":{"start":{"value":487,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023029"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20018.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20018.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000012","properties":[{"key":"ProteinId","value":"PKW20018.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A497TZX0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005694","properties":[{"key":"GoTerm","value":"C:chromosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034335","properties":[{"key":"GoTerm","value":"F:DNA negative supercoiling activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006261","properties":[{"key":"GoTerm","value":"P:DNA-templated DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd16928","properties":[{"key":"EntryName","value":"HATPase_GyrB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00822","properties":[{"key":"EntryName","value":"TopoII_Trans_DNA_gyrase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03366","properties":[{"key":"EntryName","value":"TOPRIM_TopoIIA_GyrB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000005","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.565.10:FF:000002","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.670:FF:000002","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.670","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01898","properties":[{"key":"EntryName","value":"GyrB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002288","properties":[{"key":"EntryName","value":"DNA_gyrase_B_C"}]},{"database":"InterPro","id":"IPR011557","properties":[{"key":"EntryName","value":"GyrB"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR003594","properties":[{"key":"EntryName","value":"HATPase_dom"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"InterPro","id":"IPR001241","properties":[{"key":"EntryName","value":"Topo_IIA"}]},{"database":"InterPro","id":"IPR013760","properties":[{"key":"EntryName","value":"Topo_IIA-like_dom_sf"}]},{"database":"InterPro","id":"IPR000565","properties":[{"key":"EntryName","value":"Topo_IIA_B"}]},{"database":"InterPro","id":"IPR013759","properties":[{"key":"EntryName","value":"Topo_IIA_B_C"}]},{"database":"InterPro","id":"IPR013506","properties":[{"key":"EntryName","value":"Topo_IIA_bsu_dom2"}]},{"database":"InterPro","id":"IPR018522","properties":[{"key":"EntryName","value":"TopoIIA_CS"}]},{"database":"InterPro","id":"IPR006171","properties":[{"key":"EntryName","value":"TOPRIM_dom"}]},{"database":"InterPro","id":"IPR034160","properties":[{"key":"EntryName","value":"TOPRIM_GyrB"}]},{"database":"NCBIfam","id":"TIGR01059","properties":[{"key":"EntryName","value":"gyrB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004189","properties":[{"key":"EntryName","value":"PRK05644.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011501","properties":[{"key":"EntryName","value":"PRK14939.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866:SF1","properties":[{"key":"EntryName","value":"DNA GYRASE SUBUNIT B, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866","properties":[{"key":"EntryName","value":"DNA GYRASE/TOPOISOMERASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00204","properties":[{"key":"EntryName","value":"DNA_gyraseB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00986","properties":[{"key":"EntryName","value":"DNA_gyraseB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02518","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01751","properties":[{"key":"EntryName","value":"Toprim"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01159","properties":[{"key":"EntryName","value":"DNAGYRASEB"}]},{"database":"PRINTS","id":"PR00418","properties":[{"key":"EntryName","value":"TPI2FAMILY"}]},{"database":"SMART","id":"SM00387","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00433","properties":[{"key":"EntryName","value":"TOP2c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56719","properties":[{"key":"EntryName","value":"Type II DNA topoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00177","properties":[{"key":"EntryName","value":"TOPOISOMERASE_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50880","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MWLIITPVFIYLFVKQKNTFLDRLYMSEEIKKSNYSADSIQALEGMEHVRMRPSMYIGDVGVRGLHHLVYEVVDNSIDEAMGGHCDTISVTINEDNSVTVEDNGRGIPVDIHKKEGVSALEVVMTKIGAGGKFDKDSYKVSGGLHGVGVSVVNALSNHMKSTVFRDGKIYEQEYERGKALYPVKQIGETEKRGTRQTFYPDDTIFTQTTEFSYDTLSARMRELSFLNKGITITFTDRRVKDEKGEFLSEVFHSDEGLKEYIRFLDGNREPIISHVISMESEKGEIPVEVALIYNTSYSENIFSYVNNINTHEGGTHLQGFRTGLTRSLKKYADASGLLEKLKFEITGDDFREGLTAIISVKVSEPQFEGQTKTKLGNREVVSPVSQAVGDMIEAYLEENPNDARVIVQKVILAAQARHAAKKAREMVQRKTVMGGGGLPGKLSDCSEQDPAKCEVFLVEGDSAGGTAKQGRDRNFQAILPLRGKILNVEKAMHHKVFENEEIRNIFTALGVTIGTAEDSKALNIEKLRYHKVVIMCDADVDGSHISTLILTFFFRFMKELIENGHVYIATPPLYMVKKGNKKEYAWNDAQRDEITERMGGGSSVQRYKGLGEMNAEQLWETTLNPEFRTLRQVTIDSLAEADRIFSMLMGDEVPPRREFIEKNAAYANIDA","length":671,"molWeight":75328,"crc64":"5DDAF61C17C9D82E","md5":"8369A203E79898B392AF7A2D19B5A46B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":4,"Site":2},"uniParcId":"UPI000CBAF145"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U1A2","uniProtkbId":"A0A497U1A2_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30110.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"N-acetylmuramic acid 6-phosphate etherase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"MurNAc-6-P etherase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"4.2.1.126"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"N-acetylmuramic acid 6-phosphate hydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"N-acetylmuramic acid 6-phosphate lyase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"murQ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30110.1"}],"value":"B0G92_1759"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-D-muramate 6-phosphate + H2O = N-acetyl-D-glucosamine 6-phosphate + (R)-lactate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26410"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16004"},{"database":"ChEBI","id":"CHEBI:57513"},{"database":"ChEBI","id":"CHEBI:58722"}],"ecNumber":"4.2.1.126","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Amino-sugar metabolism; N-acetylmuramate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30110.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]},{"type":"Active site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}]},{"type":"Active site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30110.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30110.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW30110.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101471809.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497U1A2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016835","properties":[{"key":"GoTerm","value":"F:carbon-oxygen lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016803","properties":[{"key":"GoTerm","value":"F:ether hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046348","properties":[{"key":"GoTerm","value":"P:amino sugar catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097173","properties":[{"key":"GoTerm","value":"P:N-acetylmuramic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009254","properties":[{"key":"GoTerm","value":"P:peptidoglycan turnover"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd05007","properties":[{"key":"EntryName","value":"SIS_Etherase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000014","properties":[{"key":"EntryName","value":"N-acetylmuramic acid 6-phosphate etherase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00068","properties":[{"key":"EntryName","value":"MurQ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005488","properties":[{"key":"EntryName","value":"Etherase_MurQ"}]},{"database":"InterPro","id":"IPR005486","properties":[{"key":"EntryName","value":"Glucokinase_regulatory_CS"}]},{"database":"InterPro","id":"IPR040190","properties":[{"key":"EntryName","value":"MURQ/GCKR"}]},{"database":"InterPro","id":"IPR001347","properties":[{"key":"EntryName","value":"SIS_dom"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00274","properties":[{"key":"EntryName","value":"N-acetylmuramic acid 6-phosphate etherase"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003915","properties":[{"key":"EntryName","value":"PRK05441.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009222","properties":[{"key":"EntryName","value":"PRK12570.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10088","properties":[{"key":"EntryName","value":"GLUCOKINASE REGULATORY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10088:SF4","properties":[{"key":"EntryName","value":"GLUCOKINASE REGULATORY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22645","properties":[{"key":"EntryName","value":"GKRP_SIS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01272","properties":[{"key":"EntryName","value":"GCKR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51464","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAFTKTTEQSSKYEHLEKMPVADLLRNINNEDKTVPLAVEKALPQIEKLVEKIVEKMKEGGRLFYIGAGTSGRLGIVDASECPPTFGVPFDLVIGIIAGGDTAIRKAVEFAEDDREQAWKDLQEWDINEKDVVIGIAASGTTPYVIGGLQKCIEKNITTGSISCNAESPLSKTSDFPIDVVVGPEFVTGSSRMKAGTAQKLVLNMISTSTMIQLGRVKGNKMVDMQLSNHKLVGRAVRMIMEELSVSETEATSLLEKYKNVRNSIENYKK","length":270,"molWeight":29602,"crc64":"EBD17B8CBA3F1558","md5":"D7D26A75D4D9E6F6EB2A49CB1732E19A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2},"uniParcId":"UPI000C701301"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U1D6","uniProtkbId":"A0A497U1D6_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20509.1"}],"value":"B0G92_2655"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20509.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000009","properties":[{"key":"ProteinId","value":"PKW20509.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472539.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000009.1"}]},{"database":"AlphaFoldDB","id":"A0A497U1D6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEALLINKHEILKRYKPVSVQAHKGTQGHALIIGGSYGKIGSIILASKASLKSGCGLVTALIPKCGYTSIQTSFPEAMVITDKEEAYISEIEFEIIPNAIAIGMGIGQHETTQKAFIKFLKNNNKPLLIDADGINILSKNKELFDFVSEQTILTPHRKELQRLIGDWSSEEEMIEKAARLTESKKWIIVIKGAPTQIISGNAIYTNSTGNQALATAGSGDTLSGIIAGLLAQGYTPEDAAILGVYIHGLTADIGSKSLGYQAFIASDIIENLGKAFLSLDENF","length":283,"molWeight":30451,"crc64":"601C70DB9035CFF7","md5":"7935D394BDFD3EFD963BAC046E19F2F7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":5},"uniParcId":"UPI000C703C3C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U1F5","uniProtkbId":"A0A497U1F5_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine dehydrogenase (decarboxylating)"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"1.4.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine cleavage system P-protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine decarboxylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine dehydrogenase (aminomethyl-transferring)"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"gcvP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20427.1"}],"value":"B0G92_3139"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003788"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[glycine-cleavage complex H protein] + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24304"},{"database":"Rhea","id":"RHEA-COMP:10494"},{"database":"Rhea","id":"RHEA-COMP:10495"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:83099"},{"database":"ChEBI","id":"CHEBI:83143"}],"ecNumber":"1.4.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049026"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603437-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011690"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"The glycine cleavage system is composed of four proteins: P, T, L and H"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010756"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Belongs to the GcvP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20427.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"Glycine cleavage system P-protein N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02347"}]},{"type":"Domain","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":727,"modifier":"EXACT"}},"description":"Glycine cleavage system P-protein N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02347"}]},{"type":"Domain","location":{"start":{"value":772,"modifier":"EXACT"},"end":{"value":889,"modifier":"EXACT"}},"description":"Glycine dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF21478"}]},{"type":"Modified residue","location":{"start":{"value":700,"modifier":"EXACT"},"end":{"value":700,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603437-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000010","properties":[{"key":"ProteinId","value":"PKW20427.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472897.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000010.1"}]},{"database":"AlphaFoldDB","id":"A0A497U1F5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005960","properties":[{"key":"GoTerm","value":"C:glycine cleavage complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016594","properties":[{"key":"GoTerm","value":"F:glycine binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004375","properties":[{"key":"GoTerm","value":"F:glycine dehydrogenase (decarboxylating) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019464","properties":[{"key":"GoTerm","value":"P:glycine decarboxylation via glycine cleavage system"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00613","properties":[{"key":"EntryName","value":"GDC-P"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000005","properties":[{"key":"EntryName","value":"Glycine dehydrogenase (decarboxylating), mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000007","properties":[{"key":"EntryName","value":"glycine dehydrogenase (Decarboxylating), mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00711","properties":[{"key":"EntryName","value":"GcvP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003437","properties":[{"key":"EntryName","value":"GcvP"}]},{"database":"InterPro","id":"IPR049316","properties":[{"key":"EntryName","value":"GDC-P_C"}]},{"database":"InterPro","id":"IPR049315","properties":[{"key":"EntryName","value":"GDC-P_N"}]},{"database":"InterPro","id":"IPR020581","properties":[{"key":"EntryName","value":"GDC_P"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR00461","properties":[{"key":"EntryName","value":"gcvP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11773:SF1","properties":[{"key":"EntryName","value":"GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11773","properties":[{"key":"EntryName","value":"GLYCINE DEHYDROGENASE, DECARBOXYLATING"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21478","properties":[{"key":"EntryName","value":"GcvP2_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02347","properties":[{"key":"EntryName","value":"GDC-P"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MKTDAFALRHIGPRENDLQHMLKTIGVESIDRLIYETLPDDIRLKAPLNLEPAMTEYEYLNHIQKLGNKNKVFKSYIGLGYHPAIVPAVIQRNIFENPGWYTAYTPYQAEIAQGRLEALLNFQTTVIELTGMEIANASLLDEGTAAAEAMALLFDVRTRDQKKNNANKFFVSEEILPQTLSVLETRSTPIGVELVVGNHEEFTFGNDFFGAILQYPGKYGQVYDYAAFIAQAKSNEIKVAVAADIMSLVKLTSPGEMGADVVVGTTQRFGIPMGYGGPHAAYFATKEEYKRSMPGRIIGVTIDTNGNRALRMALQTREQHIKREKATSNICTAQVLLAVMAGMYAVYHGPKGLDYIAGKIHASAVTTANALSKLGIEQTNSSFFDTIVVKADAQKVKAIAEKNEFNFYYIDNNTVAISFNETTGLADINTIVSIFAEAAGKETIKVAELATQTQYSESLNRTSTFLAHEVFNKHHSETALMRYIKMLERKDLALNHSMISLGSCTMKLNAAAEMLPLSMANWNNIHPFAPIEQAEGYQTMLKKLEQQLNVITGFAGTTLQPNSGAQGEYAGLMVIRAYHQSRGESHRNIALIPASAHGTNPATATMAGMQVVVTKTSENGNIDVEDLRAKAIQYKDNLACLMVTYPSTHGVYEASIIEVTKIIHENGGQVYMDGANMNAQVGLTNPATIGADVCHLNLHKTFAIPHGGGGPGVGPICVAPHLVEFLPTNPVIPTGGNHAITAISAAPWGSALVCLISYGYITMLGAEGLTSSTQHAILNANYIKERLNGHYATLYSGEMGRAAHEMIIECRPFKEKGIEVTDIAKRLMDYGFHAPTVSFPVAGTLMIEPTESENLEELDRFCDAMISIRKEIEKASADDKNNVLKNSPHTLAMLTADTWDFPYTREEAAFPLEYIAENKFWPSVRRVDDAYGDRNLVCSCAPIEAYMES","length":949,"molWeight":104066,"crc64":"B8EBC622C31D1506","md5":"A37E3DA1105DC8D5965E7261AEBDA6B6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Modified residue":1},"uniParcId":"UPI000C711B57"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U1Y5","uniProtkbId":"A0A497U1Y5_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20244.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01389"}],"value":"DNA helicase RecQ"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01389"}],"value":"5.6.2.4"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20244.1"}],"value":"B0G92_2956"}]}],"comments":[{"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:0000256","source":"ARBA","id":"ARBA00034617"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005446"}],"value":"Belongs to the helicase family. RecQ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20244.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Domain","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":614,"modifier":"EXACT"}},"description":"HRDC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50967"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20244.1"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20244.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20244.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000010","properties":[{"key":"ProteinId","value":"PKW20244.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472775.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000010.1"}]},{"database":"AlphaFoldDB","id":"A0A497U1Y5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0043590","properties":[{"key":"GoTerm","value":"C:bacterial nucleoid"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030894","properties":[{"key":"GoTerm","value":"C:replisome"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' 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:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009378","properties":[{"key":"GoTerm","value":"F:four-way junction helicase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"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:0009432","properties":[{"key":"GoTerm","value":"P:SOS response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd17920","properties":[{"key":"EntryName","value":"DEXHc_RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18794","properties":[{"key":"EntryName","value":"SF2_C_RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000156","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase recQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001051","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.1390","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.80","properties":[{"key":"EntryName","value":"HRDC domain"},{"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":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011545","properties":[{"key":"EntryName","value":"DEAD/DEAH_box_helicase_dom"}]},{"database":"InterPro","id":"IPR004589","properties":[{"key":"EntryName","value":"DNA_helicase_ATP-dep_RecQ"}]},{"database":"InterPro","id":"IPR006293","properties":[{"key":"EntryName","value":"DNA_helicase_ATP-dep_RecQ_bac"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR010997","properties":[{"key":"EntryName","value":"HRDC-like_sf"}]},{"database":"InterPro","id":"IPR002121","properties":[{"key":"EntryName","value":"HRDC_dom"}]},{"database":"InterPro","id":"IPR044876","properties":[{"key":"EntryName","value":"HRDC_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR048671","properties":[{"key":"EntryName","value":"RecQ-1-like_HTH"}]},{"database":"InterPro","id":"IPR032284","properties":[{"key":"EntryName","value":"RecQ_Zn-bd"}]},{"database":"InterPro","id":"IPR018982","properties":[{"key":"EntryName","value":"RQC_domain"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR036390","properties":[{"key":"EntryName","value":"WH_DNA-bd_sf"}]},{"database":"NCBIfam","id":"TIGR01389","properties":[{"key":"EntryName","value":"recQ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00614","properties":[{"key":"EntryName","value":"recQ_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13710:SF105","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE Q1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13710","properties":[{"key":"EntryName","value":"DNA HELICASE RECQ FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00270","properties":[{"key":"EntryName","value":"DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00570","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21220","properties":[{"key":"EntryName","value":"RecQ-1-like_HTH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16124","properties":[{"key":"EntryName","value":"RecQ_Zn_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09382","properties":[{"key":"EntryName","value":"RQC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00341","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00956","properties":[{"key":"EntryName","value":"RQC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47819","properties":[{"key":"EntryName","value":"HRDC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46785","properties":[{"key":"EntryName","value":"Winged helix' DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50967","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNSNEIDIHKELKKYFGFSQFKGLQEQVVKSIINRNNTFVIMPTGGGKSLCYQLPALIKEGTAIVVSPLIALMKNQVDAIRSLSSENGIAHVLNSSLTKTEIAQVKKDIVSGITKLLYVAPESLTKEEYIQFLKSVPLSFVAIDEAHCISEWGHDFRPEYRNLRTIIKQLGDIPVIGLTATATPKVQEDILKNLDMVNAKTFKASFNRPNLFYEVRTKTKNIESDIIRFIKQHKGKSGIIYCLSRKKVEEIAQVLQVNGISAVPYHAGLDAKTRAKHQDMFLMEDVDVVVATIAFGMGIDKPDVRFVIHHDIPKSLESYYQETGRAGRDGGEGHCLAYYSYKDVEKLEKFMAGKPVAEQEIGFALLQEVVAYAETSMSRRKFLLHYFGEEFDSETGEGADMDDNVRNPKKKVEAKDQVVKLLKIVRDTKHLYKSKEIIFTLIGKINATIKAHKTDAQSFFGSGADFDERYWMALIRQVLVDGYLSKDIETYGILKLTEKGADFIKNPASFMMSEDHDYNESEDEAIVTAAKSSGTADEVLMGMLRDLRKKVAKKLGVPPFVVFQDPSLEDMALKYPVSIEELGSVHGVGEGKAKKYGKDFVELIGRYVEDNDIIRPDDLVVKSTGANSALKLYIIQNVDRKLSLNDIAKAKGLDMDVLLKEMEQIVYSGTKLNIKYWIDDILDEDQQEEIHEYFMESDSDNIKDALKEFDGDYDIEELRLMRIKFISEVAN","length":731,"molWeight":82490,"crc64":"659B07BA056A8AF8","md5":"4CC152FD4A055A93C7FE3018967D97EC"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI000C70A261"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U1Y6","uniProtkbId":"A0A497U1Y6_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"Ribosomal protein uS12 methylthiotransferase RimO"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"uS12 MTTase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"uS12 methylthiotransferase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"2.8.4.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"Ribosomal protein uS12 (aspartate-C(3))-methylthiotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"Ribosome maturation factor RimO"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"rimO"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"}],"value":"B0G92_1488"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate(89)-[ribosomal protein uS12]-hydrogen + (sulfur carrier)-SH + AH2 + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + (sulfur carrier)-H + 5'-deoxyadenosine + L-methionine + A + S-adenosyl-L-homocysteine + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:37087"},{"database":"Rhea","id":"RHEA-COMP:10460"},{"database":"Rhea","id":"RHEA-COMP:10461"},{"database":"Rhea","id":"RHEA-COMP:14737"},{"database":"Rhea","id":"RHEA-COMP:14739"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:29917"},{"database":"ChEBI","id":"CHEBI:29961"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64428"},{"database":"ChEBI","id":"CHEBI:73599"}],"ecNumber":"2.8.4.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"value":"Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"value":"Belongs to the methylthiotransferase family. RimO subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"MTTase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51449"}]},{"type":"Domain","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Domain","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"TRAM","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50926"}]},{"type":"Binding site","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"}],"id":"KW-0687","category":"Molecular function","name":"Ribonucleoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"}],"id":"KW-0689","category":"Molecular function","name":"Ribosomal protein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01865"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW29842.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW29842.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101471618.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497U1Y6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0035599","properties":[{"key":"GoTerm","value":"F:aspartic acid methylthiotransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0103039","properties":[{"key":"GoTerm","value":"F:protein methylthiotransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006400","properties":[{"key":"GoTerm","value":"P:tRNA modification"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.80.30.20:FF:000001","properties":[{"key":"EntryName","value":"tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12160","properties":[{"key":"EntryName","value":"Methylthiotransferase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.80.30.20","properties":[{"key":"EntryName","value":"tm_1862 like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01865","properties":[{"key":"EntryName","value":"MTTase_RimO"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006638","properties":[{"key":"EntryName","value":"Elp3/MiaA/NifB-like_rSAM"}]},{"database":"InterPro","id":"IPR005839","properties":[{"key":"EntryName","value":"Methylthiotransferase"}]},{"database":"InterPro","id":"IPR020612","properties":[{"key":"EntryName","value":"Methylthiotransferase_CS"}]},{"database":"InterPro","id":"IPR013848","properties":[{"key":"EntryName","value":"Methylthiotransferase_N"}]},{"database":"InterPro","id":"IPR038135","properties":[{"key":"EntryName","value":"Methylthiotransferase_N_sf"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR005840","properties":[{"key":"EntryName","value":"Ribosomal_uS12_MeSTrfase_RimO"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR023404","properties":[{"key":"EntryName","value":"rSAM_horseshoe"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"InterPro","id":"IPR002792","properties":[{"key":"EntryName","value":"TRAM_dom"}]},{"database":"NCBIfam","id":"TIGR01125","properties":[{"key":"EntryName","value":"30S ribosomal protein S12 methylthiotransferase RimO"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00089","properties":[{"key":"EntryName","value":"MiaB/RimO family radical SAM methylthiotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43837","properties":[{"key":"EntryName","value":"RIBOSOMAL PROTEIN S12 METHYLTHIOTRANSFERASE RIMO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43837:SF1","properties":[{"key":"EntryName","value":"RIBOSOMAL PROTEIN US12 METHYLTHIOTRANSFERASE RIMO"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18693","properties":[{"key":"EntryName","value":"TRAM_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00919","properties":[{"key":"EntryName","value":"UPF0004"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01082","properties":[{"key":"EntryName","value":"B12-binding_domain_containing"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01061","properties":[{"key":"EntryName","value":"methylthiotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00274","properties":[{"key":"EntryName","value":"ribosomal_protein_S12_methylth"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00729","properties":[{"key":"EntryName","value":"Elp3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51449","properties":[{"key":"EntryName","value":"MTTASE_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01278","properties":[{"key":"EntryName","value":"MTTASE_RADICAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50926","properties":[{"key":"EntryName","value":"TRAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRTKSLKKNKINVITLGCSKNVYDSEVLMGQLRASGKDVTHEAPAHEEGNIIVINTCGFIDNAKEESVNMILNYVDKKEQGLVDKVFVTGCLSERYKPDLIKEIPNVDQYFGTTELPGLLKALGADYRHELLGERLTTTPKNYAYLKIAEGCDRPCSFCAIPLMRGKHVSQPIEKLVNEAKGLAKNGVKELILIAQDLTYYGLDLYKKRNLAELLENLAAVEGIEWIRLHYAFPTGFPMDVLELMKREPKICNYLDIPLQHISDNILKSMRRGTTQAKTTKLIEDFRNTVPGMTIRTTLIVGYPGETEEDFQILKNWVEEMRFERLGCFTYSHEENTHAYLLEDDVPAEVKQQRANEIMELQSQISWELNQEKIGQVFRCIIDRKEGNHFVGRTEFDSPDVDNEVLIDASKAYLKTGEFVNVRITDAAEFDLYGEAVL","length":438,"molWeight":49856,"crc64":"4D2B268462D9983D","md5":"1A0A313F4748A17751313F243755A4C2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Binding site":9},"uniParcId":"UPI000C712552"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U2C2","uniProtkbId":"A0A497U2C2_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20504.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"DNA gyrase subunit A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"5.6.2.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"gyrA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20504.1"}],"value":"B0G92_2647"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent breakage, passage and rejoining of double-stranded DNA.","ecNumber":"5.6.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01384"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008263"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"value":"Belongs to the type II topoisomerase GyrA/ParC subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20504.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"Topo IIA-type catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS52040"}]},{"type":"Region","location":{"start":{"value":816,"modifier":"EXACT"},"end":{"value":844,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Motif","location":{"start":{"value":523,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"GyrA-box","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}]},{"type":"Compositional bias","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":844,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01384"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023029"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01897"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20504.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20504.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000009","properties":[{"key":"ProteinId","value":"PKW20504.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472535.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALHAS010000010.1"}]},{"database":"AlphaFoldDB","id":"A0A497U2C2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005694","properties":[{"key":"GoTerm","value":"C:chromosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009330","properties":[{"key":"GoTerm","value":"C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034335","properties":[{"key":"GoTerm","value":"F:DNA negative supercoiling activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006261","properties":[{"key":"GoTerm","value":"P:DNA-templated DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00187","properties":[{"key":"EntryName","value":"TOP4c"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.268.10:FF:000001","properties":[{"key":"EntryName","value":"DNA gyrase subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.199.10:FF:000001","properties":[{"key":"EntryName","value":"DNA gyrase subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.120.10.90:FF:000005","properties":[{"key":"EntryName","value":"DNA topoisomerase 4 subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1360.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.120.10.90","properties":[{"key":"EntryName","value":"DNA gyrase/topoisomerase IV, subunit A, C-terminal"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.199.10","properties":[{"key":"EntryName","value":"Topoisomerase II, domain 5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.268.10","properties":[{"key":"EntryName","value":"Topoisomerase, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01897","properties":[{"key":"EntryName","value":"GyrA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005743","properties":[{"key":"EntryName","value":"GyrA"}]},{"database":"InterPro","id":"IPR006691","properties":[{"key":"EntryName","value":"GyrA/parC_rep"}]},{"database":"InterPro","id":"IPR035516","properties":[{"key":"EntryName","value":"Gyrase/topoIV_suA_C"}]},{"database":"InterPro","id":"IPR013760","properties":[{"key":"EntryName","value":"Topo_IIA-like_dom_sf"}]},{"database":"InterPro","id":"IPR013758","properties":[{"key":"EntryName","value":"Topo_IIA_A/C_ab"}]},{"database":"InterPro","id":"IPR013757","properties":[{"key":"EntryName","value":"Topo_IIA_A_a_sf"}]},{"database":"InterPro","id":"IPR002205","properties":[{"key":"EntryName","value":"Topo_IIA_dom_A"}]},{"database":"InterPro","id":"IPR050220","properties":[{"key":"EntryName","value":"Type_II_DNA_Topoisomerases"}]},{"database":"NCBIfam","id":"NF004043","properties":[{"key":"EntryName","value":"gyrA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01063","properties":[{"key":"EntryName","value":"gyrA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004044","properties":[{"key":"EntryName","value":"PRK05561.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43493:SF5","properties":[{"key":"EntryName","value":"DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43493","properties":[{"key":"EntryName","value":"DNA GYRASE/TOPOISOMERASE SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03989","properties":[{"key":"EntryName","value":"DNA_gyraseA_C"},{"key":"MatchStatus","value":"6"}]},{"database":"Pfam","id":"PF00521","properties":[{"key":"EntryName","value":"DNA_topoisoIV"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00434","properties":[{"key":"EntryName","value":"TOP4c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101904","properties":[{"key":"EntryName","value":"GyrA/ParC C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56719","properties":[{"key":"EntryName","value":"Type II DNA topoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS52040","properties":[{"key":"EntryName","value":"TOPO_IIA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAEGEKLIPINIEDEMKSSYIDYSMSVIVSRALPDVRDGLKPVHRRVLYGMYELGVFSNRAHKKSARIVGEVLGKYHPHGDTSVYDAMVRMAQEWSLRYLLVDGQGNFGSVDGDSPAAMRYTEARMRKIAEEIMADIDKETVDFQLNFDDTLEEPKVMPTKVPTLLINGASGIAVGMATNMAPHNLSEVVDGTLAYIDNNDIEIDELMHHIKAPDFPTGGTIYGYEGVREAFKTGRGRIVMRAKVNFEEVDGRECIVVTEIPYQVNKADMIKKTADLVNEKKIDGISNIRDESDRNGMRIVYILRRDAVPNVVLNTLYKYTQLQSSFSVNNIALVNGRPQLLNLKDLIHHFVEHRHEVVTRRAQYELRKAEERAHILEGLIIASDNIDEVIQLIRSSSNTDEAREKLIARFNLSEIQAKAIVEMRLRQLTGLEQDKLRAEYEEIMKLIAHLKELLASKEMRMALIKEELTEIKDKYGDERRSTIEYSGGDVSIEDLIADENVVITISHAGYIKRTNLSEYKTQNRGGVGQKGVATRDQDFLEHLFVATNHQYMMFFTQKGKCFWMRVYEIPEGTKTSKGRAIQNLINIENDDKVKAFICTQDLKNQDYINSHYVIMATKQGQVKKTLLEQYSRPRVNGIAAITIKEDDELLEAKLTNGESQILIAVKSGKLVRFEENKTRPMGRSASGVRGITLGHEKDEVIGMVSVNDMESEILVVSENGYGKRSSLEDYRITNRGGKGVKTLNITDKTGELISINNVTDADDLMIINKSGLTIRMEVSDLRVMGRATQGVRLINIKGNDSIAAVTKVIREEQVIDETEGDGENTALEASTNDDVTEVENTEE","length":844,"molWeight":95070,"crc64":"E6DAE983B868D7FD","md5":"4B89B0FE4CDF7F2F0209F74F4936C058"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Coiled coil":1,"Motif":1,"Compositional bias":1,"Active site":1},"uniParcId":"UPI000C7152E1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U2E3","uniProtkbId":"A0A497U2E3_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30022.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Dihydroorotate dehydrogenase (quinone)"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"1.3.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"DHOdehase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"DHOD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"DHODase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Dihydroorotate oxidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"pyrD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30022.1"}],"value":"B0G92_1671"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + a quinone = orotate + a quinol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30187"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:30864"},{"database":"ChEBI","id":"CHEBI:132124"}],"ecNumber":"1.3.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048639"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Binds 1 FMN per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005161"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30022.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Dihydroorotate dehydrogenase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01180"}]},{"type":"Active site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}]},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30022.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30022.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW30022.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101471748.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497U2E3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0106430","properties":[{"key":"GoTerm","value":"F:dihydroorotate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04738","properties":[{"key":"EntryName","value":"DHOD_2_like"},{"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_00225","properties":[{"key":"EntryName","value":"DHO_dh_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR050074","properties":[{"key":"EntryName","value":"DHO_dehydrogenase"}]},{"database":"InterPro","id":"IPR012135","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_1_2"}]},{"database":"InterPro","id":"IPR005719","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_2"}]},{"database":"InterPro","id":"IPR005720","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_cat"}]},{"database":"InterPro","id":"IPR001295","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_CS"}]},{"database":"NCBIfam","id":"NF003645","properties":[{"key":"EntryName","value":"PRK05286.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003652","properties":[{"key":"EntryName","value":"PRK05286.2-5"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01036","properties":[{"key":"EntryName","value":"pyrD_sub2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48109:SF4","properties":[{"key":"EntryName","value":"DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48109","properties":[{"key":"EntryName","value":"DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01180","properties":[{"key":"EntryName","value":"DHO_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000164","properties":[{"key":"EntryName","value":"DHO_oxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00912","properties":[{"key":"EntryName","value":"DHODEHASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYKSVIRPILFGFDPEKIHYFTFSTLRFLNKIPGASSVFKSLYQVDNKRLEREVFGLKFKNPVGLAAGFDKDAKLYKELSNLGFGFIEIGTLTPKGQEGNPKKRLFRLKEDSAIINRMGFNNGGVFEAVERLKKNNGVLIGGNIGKNKLTPNEDAVSDYEICFDALYDYVDYFVVNVSSPNTPNLRALQDKEPLTQLLQTLQQKNTTKPKQKPILLKIAPDLTDEQLLDIVDIVNDTKIAGVIATNTTISREGLISENQKETGGLSGKPLTKRSTEVIRFLSEKSNKSFPIIGVGGIHSAEDALEKLEAGASLVQLYTGFIYEGPALIKKINKKILSKK","length":339,"molWeight":37680,"crc64":"D666695A8178C023","md5":"1F5B450D4890A97CDEACE3555090A034"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":14},"uniParcId":"UPI000C7113E5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U2K5","uniProtkbId":"A0A497U2K5_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-06-05","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30092.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Phosphoserine aminotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"2.6.1.52"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Phosphohydroxythreonine aminotransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"PSAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"serC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30092.1"}],"value":"B0G92_1741"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-(phosphooxy)-L-threonine + 2-oxoglutarate = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16573"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58452"},{"database":"ChEBI","id":"CHEBI:58538"}],"ecNumber":"2.6.1.52","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14329"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:18110"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57524"}],"ecNumber":"2.6.1.52","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049007"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Binds 1 pyridoxal phosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005099"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004915"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30092.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Aminotransferase class V","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00266"}]},{"type":"Binding site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29985"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"L-glutamate","id":"ChEBI:CHEBI:29985"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Modified residue","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023096"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0664","category":"Biological process","name":"Pyridoxine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023299"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0718","category":"Biological process","name":"Serine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00160"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30092.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW30092.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000007","properties":[{"key":"ProteinId","value":"PKW30092.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101471799.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_PJND01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A497U2K5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004648","properties":[{"key":"GoTerm","value":"F:O-phospho-L-serine:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006564","properties":[{"key":"GoTerm","value":"P:L-serine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008615","properties":[{"key":"GoTerm","value":"P:pyridoxine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.640.10:FF:000010","properties":[{"key":"EntryName","value":"Phosphoserine aminotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000006","properties":[{"key":"EntryName","value":"Phosphoserine aminotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00160","properties":[{"key":"EntryName","value":"SerC_aminotrans_5"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000192","properties":[{"key":"EntryName","value":"Aminotrans_V_dom"}]},{"database":"InterPro","id":"IPR020578","properties":[{"key":"EntryName","value":"Aminotrans_V_PyrdxlP_BS"}]},{"database":"InterPro","id":"IPR022278","properties":[{"key":"EntryName","value":"Pser_aminoTfrase"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"NF003764","properties":[{"key":"EntryName","value":"serC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43247","properties":[{"key":"EntryName","value":"PHOSPHOSERINE AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43247:SF1","properties":[{"key":"EntryName","value":"PHOSPHOSERINE AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00266","properties":[{"key":"EntryName","value":"Aminotran_5"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000525","properties":[{"key":"EntryName","value":"SerC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00595","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKHNYSAGPCILPQEVFEKSAQAILNFNDSGLSILEISHRSKDFVAVMEEARALVLELLGLQGKGYQALFLQGGASMEFLRVPYNLLRDGGKASYLDTGTWAAGAIKEAKAFGETIVVASSKEDKYNHIPKHYAIPADADYFHCTSNNTIYGTQIKEFPETKIPVVCDMSSDIFSRQLDFSKFDLIYAGAQKNMGPAGVTLVVVKEAILGKTGRNIPNILNYQQHIEKESMYNTPAVFAVYTSLLTLQWLKRQGGIPAIEKINEAKAQLLYAEIDRNPLFNGTAVTEDRSNMNATFLLKDETQAQAFDQYWKEAGISGLTGHRSVGGYRASMYNALPLESVQVLVDVMKEFEKTNA","length":357,"molWeight":39547,"crc64":"5E09265A74DD8BEE","md5":"B55FC073EB60A2D3CFCC5194D3DD5042"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":7,"Modified residue":1},"uniParcId":"UPI000C7021FC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A497U3E2","uniProtkbId":"A0A497U3E2_9FLAO","entryAudit":{"firstPublicDate":"2019-06-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-06-05","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Flavobacterium lindanitolerans","taxonId":428988,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20089.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Flavobacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"2.7.1.71"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"aroK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20089.1"}],"value":"B0G92_3165"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20089.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-754CGANN878Q1","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of soil and plant-associated and newly described type strains.","publicationDate":"DEC-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20089.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}],"value":"IP-10","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKW20089.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000233767"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"PJND01000011","properties":[{"key":"ProteinId","value":"PKW20089.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_101472920.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBCNKL010000010.1"}]},{"database":"AlphaFoldDB","id":"A0A497U3E2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000233767","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"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":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"PANTHER","id":"PTHR21087","properties":[{"key":"EntryName","value":"SHIKIMATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21087:SF16","properties":[{"key":"EntryName","value":"SHIKIMATE KINASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIKIVLLGYMGSGKSTIAHLLSEKTQIEAFDLDKIIEERAGLSIKNIFEQKGEVFFRKLENQIFKEFISSEKDMILSLGGGTPCYANNHELLNGGGVVSFYLKASIETLYERLLSVRDNRPLIAEQEKEEMKEYIAKHLFDRSYYYNQATHIVSVDKKTPEEVTAEISRILA","length":172,"molWeight":19629,"crc64":"E9DA269B21B3A3ED","md5":"175663B8B406B24BEA9560756BECC0F7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Binding site":7},"uniParcId":"UPI000C70D2CF"}}]}