{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZYN1","uniProtkbId":"A0A368ZYN1_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX02061.1"}],"value":"DES35_10532"}]}],"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":"RCX02061.1"}],"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":3,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO: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":72,"modifier":"EXACT"},"end":{"value":73,"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":102,"modifier":"EXACT"},"end":{"value":105,"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":103,"modifier":"EXACT"},"end":{"value":103,"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":126,"modifier":"EXACT"},"end":{"value":128,"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":155,"modifier":"EXACT"},"end":{"value":155,"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":163,"modifier":"EXACT"},"end":{"value":163,"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":170,"modifier":"EXACT"},"end":{"value":172,"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":186,"modifier":"EXACT"},"end":{"value":188,"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":212,"modifier":"EXACT"},"end":{"value":212,"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":214,"modifier":"EXACT"},"end":{"value":216,"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":223,"modifier":"EXACT"},"end":{"value":223,"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":247,"modifier":"EXACT"},"end":{"value":247,"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":253,"modifier":"EXACT"},"end":{"value":256,"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":"UP000253517"}],"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-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000005","properties":[{"key":"ProteinId","value":"RCX02061.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037359937.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000004.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZYN1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000253517","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":"MKRIGVFTSGGDAPGMNACIRAAVRTALSRGLEVFGIYRGYQGMIEGDIVPMNSGDVSNIIQRGGTILKTARSDDFRTEQGRRKAAENLRKYGIEGLVCIGGDGSFKGASILYEEHGIKTIGAPGTIDNDLYGTDSTIGYDTAVNTVVQAVDKLRDTAASHNRLFIVEVMGRDAGFIALRSGIACGAEAILVPETPTYIDALIQKLRDGWNRQKHSSIVIVAEGDESGGAYEVAKAVKQNFDRYDVRVTVLGHIQRGGSPSAYDRVLASEMGYAAVEGLLDGKFNAMVGRQGREIVFVPFEKAIKHNKELNKHLLQIAATLSI","length":323,"molWeight":34799,"crc64":"C1DDF1305FC2D03F","md5":"381962E39AB396F9143D9E0B5337CED7"},"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":15},"uniParcId":"UPI0004E61429"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A2B5","uniProtkbId":"A0A369A2B5_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-11-07","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03349.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX03349.1"}],"value":"DES35_103234"}]}],"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":"ARBA","id":"ARBA00061570"},{"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":"RCX03349.1"}],"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":37,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Transmembrane","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":655,"modifier":"EXACT"},"end":{"value":697,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":655,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":676,"modifier":"EXACT"},"end":{"value":686,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":264,"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":480,"modifier":"EXACT"},"end":{"value":480,"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":484,"modifier":"EXACT"},"end":{"value":484,"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":555,"modifier":"EXACT"},"end":{"value":555,"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":"RCX03349.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03349.1"}],"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":"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":"UP000253517"}],"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-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03349.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03349.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000003","properties":[{"key":"ProteinId","value":"RCX03349.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366338.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000003.1"}]},{"database":"AlphaFoldDB","id":"A0A369A2B5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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":"1.20.58.760:FF:000003","properties":[{"key":"EntryName","value":"AFG3-like AAA ATPase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"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":"MAQKKKPQPGFGQFRKKSGPNPNEQGKPDGERGFNFYWIYIILIAIIFGIQLIGMMNTTAKKGSFNELTEYLAKGDVERIRVINSKEIQVFLKQESIREKEEFEDLRAKSTGSGVVPGPHIVFQMPADAFRDELRSFYDDNEHLDRRKVPVTYEERKDYWSDILAWVLPFLFIFLIWMFIMRRMSTMGGGPGGQIFNIGKSRAQLFDKNTNVKVTFKDVAGMEGAKEEIQEIVNFLKNPEKYTNLGGKIPKGALLAGPPGTGKTLLAKAVAGEAKVPFFSLSGSDFVEMFVGVGASRVRDLFKQAKEKAPSIIFIDEIDAIGRARGKASFSGGNDERENTLNQLLTEMDGFQTNETVIVLAATNRPEILDRALTRAGRFDRTIYIDLPDLNERKEIFKIHLRRIKYAQDLDIDFLAKQTPGFSGADIANVCNEAALIAARKDKKVVELQDFLDAVDRIVAGLEKKSRIITPEEKKVIAYHEAGHATVSWMLEHAAPLVKVTIVPRGRSLGAAWYLPEERQITTAEQIEDEMCAALGGRAAEQVIFNKISTGALSDLEKVTRQAHAMVTIFGLNEKIGNITYYDSSGQNEFGFSKPYSERTAEIIDQEVKKIIDKQYQRAIEILTENREKLSKLAELLLEKEVIFRQDLEQIFGRRKWDKDQNSEQKTENTSAENGHAPESDKKDSEEVTSDVAVRNA","length":697,"molWeight":78471,"crc64":"CA608BAAD1BB8C09","md5":"F89CEAD015CE57A3206857B2AC708480"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Transmembrane":2,"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":4},"uniParcId":"UPI000DF3B4D1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A324","uniProtkbId":"A0A369A324_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX03605.1"}],"value":"DES35_10254"}]}],"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":"RCX03605.1"}],"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":106,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"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":124,"modifier":"EXACT"},"end":{"value":124,"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":127,"modifier":"EXACT"},"end":{"value":127,"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":171,"modifier":"EXACT"},"end":{"value":172,"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":203,"modifier":"EXACT"},"end":{"value":203,"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":226,"modifier":"EXACT"},"end":{"value":228,"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":302,"modifier":"EXACT"},"end":{"value":302,"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":"UP000253517"}],"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-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000002","properties":[{"key":"ProteinId","value":"RCX03605.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A369A324","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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":"MFNCRNFVAVKPDLRSLSSDKLYQYIASLGEKPFRARQIESWLWQKNCTDFSQMSDLPKSLRERISQDFAIHPVQVDQIQRSVDGTIKNAVRLPDGMVVESVLIPTDTRITACISSQVGCSLDCRFCATARLKRMRNLDPQEIYDQVLTIRQQAEYYLERPLTNIVFMGMGEPLLNYSNVLRAIDRITSPSGLGMSPKRITLSTVGIVKMIKTLADDNPGVKLAVSLHSAIEEVRSRIMPINRTNDLTSLTDALQYWYFKTRSKVTFEYVVWKNINDRDEDINALVKLCKKIPSKVNLIEYNAIGDPNFEQAEPERINAYLTALAHHGIVAKIRRSRGKDIDAACGQLANKNDVAPEIPKKRIPETL","length":367,"molWeight":41650,"crc64":"C0772D0DCC901420","md5":"D0C2EEE1D9343AB58EEF937BC4948DA9"},"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":"UPI000E050537"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A355","uniProtkbId":"A0A369A355_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-11-07","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01904.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX01904.1"}],"value":"DES35_1062"}]}],"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":"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":"ARBA00008392"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00985"}],"value":"Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family"}],"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":"RCX01904.1"}],"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":"RCX01904.1"}],"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":"UP000253517"}],"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-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01904.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01904.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000006","properties":[{"key":"ProteinId","value":"RCX01904.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366513.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000001.1"}]},{"database":"AlphaFoldDB","id":"A0A369A355","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00046","properties":[{"key":"RectionId","value":"UER00506"}]},{"database":"Proteomes","id":"UP000253517","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":"3.40.640.10: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:SF102","properties":[{"key":"EntryName","value":"2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL"},{"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":"MYGTLKTRLREELKSIEEAGLYKKERIITSPQGAEITLSTGQKVLNFCANNYLGLSSHPKVLEAAHKALETHGFGMSSVRFICGTQDLHKELEEKISKFLGTEDTILYAAAFDANGGVFEPLFNELDAIISDELNHASIIDGVRLCKAKRYRYKNNDMNDLEAKLKEANQEGARNKIIVTDGVFSMDGFIAQLDEIVKLAEQYDALIMIDECHSTGFIGPTGRGTHEFHNVMGKIDIITSTLGKALGGAMGGFTSGRKEIIDMLRQRSRPYLFSNSLMPAIVGASIAILDMLSETTELRDKVMRNAAYFRSKMTEEGFDIKPGIHPITPVMLYDARLSQLMADELLNEGIYVIGFFYPVVPRDQARIRVQLSAAHETGHIDRAVEAFVRVGKKFNVI","length":397,"molWeight":44165,"crc64":"11456956903D1280","md5":"B64F269852CED6FF44F67919EC3BC910"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":5,"Modified residue":1},"uniParcId":"UPI000DF19B28"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A3W1","uniProtkbId":"A0A369A3W1_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03885.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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_00406"}],"value":"fabZ"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}],"value":"lpxC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03885.1"}],"value":"DES35_102341"}]}],"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":"RCX03885.1"}],"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":364,"modifier":"EXACT"},"end":{"value":364,"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":"UP000253517"}],"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-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03885.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03885.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000002","properties":[{"key":"ProteinId","value":"RCX03885.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037357605.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000002.1"}]},{"database":"AlphaFoldDB","id":"A0A369A3W1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00359","properties":[{"key":"RectionId","value":"UER00478"}]},{"database":"Proteomes","id":"UP000253517","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":"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":"MAKQRTIARPITFEGIGLHTGHKVTMTLYPADVNKGLCFKRTDLPQQIAIPALANFVSSTDRGTALKKENTVIYTVEHILAALSGCEIDNCEIHLNGPEPPIMDGSAWPFVEKILETGIVEQDEEISYYEIIDVIKFQDRQKGIEIIALPADEFQVTVLVDYETKVLGTQNAVMEKITDFPSEIAKARTFSFLHELEYLLDNGLIKGGDLNNAIVYVDKKPSEETMAKLQKAFGKKKVSVTENGILDNLELYYPNEAARHKLLDVIGDLTLCGRKIKGHIIAKRPGHKANTEFAKILFTKIKQEKSQAPKYDPNQPPVKDVVEIMKMLPHRPPFLLVDKIIYLDNVSVVGVKSVTMNEPFFVGHFPGAPVMPGVLQVEAMAQVGGIFALSTVPDPHNYLTYFLKLDEVKFKQKVVPGDTLLFKLQLLEPIRRGIVRMRGEAFVGNKLVMEAQLTAQIVKERND","length":463,"molWeight":51777,"crc64":"E801FA1D97943C66","md5":"9A3E8E2D284AA3BC170C1C1979AB8962"},"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":"UPI0004E792B2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A5V7","uniProtkbId":"A0A369A5V7_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03726.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX03726.1"}],"value":"DES35_102179"}]}],"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":"RCX03726.1"}],"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":8,"modifier":"EXACT"},"end":{"value":282,"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":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":251,"modifier":"EXACT"},"end":{"value":251,"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":257,"modifier":"EXACT"},"end":{"value":260,"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":"UP000253517"}],"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-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03726.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03726.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000002","properties":[{"key":"ProteinId","value":"RCX03726.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366107.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000002.1"}]},{"database":"AlphaFoldDB","id":"A0A369A5V7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000253517","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":"MLKIPSHIAVLTSGGDAPGMNAAIRAVVRSAVYYGKKITGIYNGYEGLINGNFQELNSRSVKYILNQGGTFLKSARSDRFRTPEGRKQAYDNLAKTGIDALIVIGGDGSFTGAKIFSEEYDFQVIGVPGTIDNDLYGTDFTIGYDTATNTAIECIDKIRDTASSHDRLFLVEVMGRDSGFIALRSAIAAGALDVIMPENDTTYDHLVETINRAGKNKKFSNIIVVAEGNKLGNIFEISNFLKGKFPHLDIKVTILGHLQRGGSPTVYDRVLASKLGVAAVEGLLIGRNKVMAGVMHQQIIYTPFEEAITRKAYINPELIRINKILTI","length":327,"molWeight":35641,"crc64":"A78661E5CF94554B","md5":"7644DF1775A28B99B3E8A256651FFEA3"},"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":13},"uniParcId":"UPI000DF2D6FA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A627","uniProtkbId":"A0A369A627_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03868.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03868.1"}],"value":"DES35_102324"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This 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"},{"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"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":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"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":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"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_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03868.1"}],"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":216,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"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":323,"modifier":"EXACT"},"end":{"value":323,"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":372,"modifier":"EXACT"},"end":{"value":372,"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":406,"modifier":"EXACT"},"end":{"value":410,"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":435,"modifier":"EXACT"},"end":{"value":435,"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":436,"modifier":"EXACT"},"end":{"value":436,"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":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"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":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"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:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03868.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX03868.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000002","properties":[{"key":"ProteinId","value":"RCX03868.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037357380.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000002.1"}]},{"database":"AlphaFoldDB","id":"A0A369A627","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0005524","properties":[{"key":"GoTerm","value":"F:ATP 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:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"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":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"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":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-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"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKILSAEQIREADRYTIQNRPIASIDLMEAAASAWVETFLQSLLYSHRKSIIIVCGPGNNGGDGLAIARMLKPLNNVTVYLMPSDNYSPDNLANQQRLRESGIQPLLLHTTDILTLPPDAVLIDALYGSGLNRPLTGLSADIVRKINASGVPVAAVDLPSGMFADSNDHNTLHTIVKASLTITFHLPKLALLMMPTGELAGEIKIVNIGLDSSFIDQQESPHHLQDADSVKVLYRPRSLWMHKGQAGRGLLIGGIGHTAGAVLLASSAALRSGIGLLYTACGLRAAQALPVHRPEAIALDLNETDLPDLVSSLEPDAIAIGPGLGTSQASAELLNEILEYPIPTVLDADALNLIAKHRWLHRLGPNHLITPHPKEALRLFGQAKPFEFHQNLLKFSQSSKTVIAFKGRFTRIYTPEGIVWFNNSGNHGMATAGSGDVLTGVLLALLAAGYPVAQAARLGVWLHGAAGDAALLRLNSPESLIAGDIINHLHQAFHQLSSST","length":500,"molWeight":53551,"crc64":"A33A2CBE7FBAAC5D","md5":"19F75EAE640705CE14CEFC73516A5D2E"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI0004E7A350"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A8V5","uniProtkbId":"A0A369A8V5_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-11-07","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX04746.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX04746.1"}],"value":"DES35_10116"}]}],"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":"RCX04746.1"}],"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":25,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":408,"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":114,"modifier":"EXACT"},"end":{"value":120,"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":156,"modifier":"EXACT"},"end":{"value":157,"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":183,"modifier":"EXACT"},"end":{"value":183,"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":191,"modifier":"EXACT"},"end":{"value":191,"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":381,"modifier":"EXACT"},"end":{"value":381,"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":405,"modifier":"EXACT"},"end":{"value":408,"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":458,"modifier":"EXACT"},"end":{"value":458,"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":462,"modifier":"EXACT"},"end":{"value":462,"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":223,"modifier":"EXACT"},"end":{"value":223,"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":"RCX04746.1"}],"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":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX04746.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX04746.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000001","properties":[{"key":"ProteinId","value":"RCX04746.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114365489.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000001.1"}]},{"database":"AlphaFoldDB","id":"A0A369A8V5","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"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":"MKIIKDLLYKVNLKGVKGNVHHTIADIASDSRLVSPGSMFVAIRGSQSDGHLFIEQAIQAGATAIVCESDYGYTEKYPNTSFFFVENSARALGLIASNFYDNPSESIKIVAVTGTNGKTTVTTQLYEVFKKMGYKCGLISTVKVMIGHDEQPATHTTPDALSLQKHLAEMHKQGIEYCFMEASSHGIHQERLVGTHLTGAVFTNITHDHLDYHKTFANYLAAKQKLFNELPSKAFALYNADDRNGAIMVQNTRARRYSYAIKQMADFHCKVIENNIGGLTIRIGGADVYTTLTGVFNAYNLLAVYATAVLLGADDSLALMAISSLSPVAGRFETITGPNGIVAIVDYAHTPDALLNVLQTLRESIKTSQQIITVMGCGGDRDKAKRPLMGKVAADWSDKVIITSDNPRSENPQAIIDEIEQGIDYHLRKKCHKIADRKEAIRLALSMANPGDVVLVAGKGHEKFQEIKGVKHPFDDKEVILQYFNE","length":486,"molWeight":53416,"crc64":"A1D79C109CDCF4B8","md5":"A77ECAC18A20BE603ACDF2B85B3FEA92"},"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":"UPI000DF36415"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369A9G8","uniProtkbId":"A0A369A9G8_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-11-07","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX05048.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX05048.1"}],"value":"DES35_101327"}]}],"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":"RCX05048.1"}],"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":2,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":395,"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":189,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"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":289,"modifier":"EXACT"},"end":{"value":289,"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":305,"modifier":"EXACT"},"end":{"value":308,"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":324,"modifier":"EXACT"},"end":{"value":324,"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":338,"modifier":"EXACT"},"end":{"value":338,"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":342,"modifier":"EXACT"},"end":{"value":342,"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":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX05048.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX05048.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000001","properties":[{"key":"ProteinId","value":"RCX05048.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037357999.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000001.1"}]},{"database":"AlphaFoldDB","id":"A0A369A9G8","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000253517","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":"MLSGKKILLGITGGIAAYKSAFLARLLVKEGADVQVVLTPGALDFITPLTLSALTGRPVYVHSHDTTTGQWYNHVELGLWADAMVIAPATTNTLAKMAHGHCDNFLLACYLSARCPVFFAPAMDLDMYAHPAVQHSIQTLQTFGCHLIDSESGPLASGLSGKGRMAEPETILAHLQDYFRKRTSLSGKTVLINGGPTYEHIDPVRFIGNHSSGDTAVYLAREAHSRGARVTLVLGPTRYTSHTFPFEVVHVTSALQMHTECLARAASADVIICAAAVADYRPAEYQINKIKKNQDSLSIQLVKNPDILADLCQSKKAHQHIIGFALETENLTQNALTKLHQKKADAIIANSPGPHTGFATPTNQVTILYSDGTIHQSSLVLKNKLASWIWDHISEHFQISQ","length":401,"molWeight":43604,"crc64":"F8F50BA0671AB187","md5":"CC139C98A41953FED1C32FDEAB53FDFE"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI0004E690EE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A369ADX7","uniProtkbId":"A0A369ADX7_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX05634.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX05634.1"}],"value":"DES35_101922"}]}],"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":"RCX05634.1"}],"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":6,"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":16,"modifier":"EXACT"},"end":{"value":16,"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":16,"modifier":"EXACT"},"end":{"value":16,"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":17,"modifier":"EXACT"},"end":{"value":22,"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":57,"modifier":"EXACT"},"end":{"value":57,"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":74,"modifier":"EXACT"},"end":{"value":74,"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":74,"modifier":"EXACT"},"end":{"value":74,"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":144,"modifier":"EXACT"},"end":{"value":144,"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":151,"modifier":"EXACT"},"end":{"value":153,"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":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX05634.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX05634.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000001","properties":[{"key":"ProteinId","value":"RCX05634.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037356629.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000001.1"}]},{"database":"AlphaFoldDB","id":"A0A369ADX7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000253517","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:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"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":"MSSATKYIFVTGGVTSSLGKGIISSSLATLLQSRGYSVTIQKLDPYINVDPGTLNPYEHGECFVTEDGAETDLDLGHYERFLNRPTSRANNVTTGRIYLNVIEKERRGEFLGKTVQVIPHITDEIKNHIKILGQSGEYEIVITEIGGTVGDIEALPYIEAVRQLKWELGENALVVHLTLIPYLKATGELKTKPTQHSVKMLQESGVQPDILVCRTEHPLGEDIRKKLALFCNVKKDAVIESIDAETIYAVPMLMRNEKLDEAVLKRLKLPMQGEPDLAQWKDFLYRLKFPKAEVTVGLIGKYVELKDSYKSIAESLIHAGAKTELKVNIRWIHAETLRPDTVSETLQGLHGVLVAPGFGERGFDGKLEAVRYARERKIPFFGICLGMQVAVIEFARNVAGLVGANSTEIDPNTPHPVIDLMEDQKNITDKGGTMRLGAWPCTLKENTLAYAIYRRTNISERHRHRYEFNNTYRNQLEEAGLVFSGVNPDKDLVEIVELTDHSFFIGVQFHPEYKSTVAHPHPLFVNFLKACDTVAKSSKD","length":540,"molWeight":60458,"crc64":"A854F21B76786001","md5":"D43A6B92F450023EBC6A062A81BB31FB"},"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":"UPI0004E6CF31"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZW88","uniProtkbId":"A0A368ZW88_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2018-11-07","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01205.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"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":"RCX01205.1"}],"value":"DES35_10718"}]}],"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":"RCX01205.1"}],"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":341,"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":65,"modifier":"EXACT"},"end":{"value":69,"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":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"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":114,"modifier":"EXACT"},"end":{"value":118,"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":271,"modifier":"EXACT"},"end":{"value":271,"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":300,"modifier":"EXACT"},"end":{"value":300,"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":321,"modifier":"EXACT"},"end":{"value":322,"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":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01205.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01205.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000007","properties":[{"key":"ProteinId","value":"RCX01205.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366543.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000003.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZW88","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00946"}]},{"database":"Proteomes","id":"UP000253517","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":"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":"PS00911","properties":[{"key":"EntryName","value":"DHODEHASE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYTLIKNLLFLLDPERAHYMAMDSLKLARQLPGGELLLRLLFNAEEFRPFEWKGLTFRHPVGLAAGFDKDGRYLRELACLGFSFIEAGTVTPLPQPGNAKPRLFRLPKDQGLINRMGFNNRGVVELRSRLLRSRPKGMVIGGNIGKNKLTPNEEAQRDYLTCFEALHDQVDYFTINVSSPNTPGLRDLQEKKPLENIITALKRHPLQREKYRPILLKIAPDLTEGQVDDLLEVMHNTGLDGVVATNTTISRDGLKTPADRLKAIGAGGLSGAPLRERSDRILSQLAKGLPQEVLLIGVGGIFEAEDVRRKLDLGAHLVQVYTGFVYEGPTLVKRMIKELKSNGKN","length":345,"molWeight":38542,"crc64":"D5650E9D45BDB7B7","md5":"50B594CA13BFA8A4BF0A2843681FDA45"},"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":"UPI000DF18428"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZYF9","uniProtkbId":"A0A368ZYF9_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02070.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097645"}],"value":"Bifunctional phosphoglucose/phosphomannose isomerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011956"}],"value":"5.3.1.8"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011952"}],"value":"5.3.1.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097797"}],"value":"Glucose-6-phosphate isomerase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097804"}],"value":"Mannose-6-phosphate isomerase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02070.1"}],"value":"DES35_10541"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-mannose 6-phosphate = D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12356"},{"database":"ChEBI","id":"CHEBI:58735"},{"database":"ChEBI","id":"CHEBI:61527"}],"ecNumber":"5.3.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000757"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029321"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010523"}],"value":"Belongs to the PGI/PMI family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02070.1"}],"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":164,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00797"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02070.1"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02070.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02070.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000005","properties":[{"key":"ProteinId","value":"RCX02070.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037359920.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000004.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZYF9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0004347","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004476","properties":[{"key":"GoTerm","value":"F:mannose-6-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:1901135","properties":[{"key":"GoTerm","value":"P:carbohydrate derivative metabolic 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":"CDD","id":"cd05017","properties":[{"key":"EntryName","value":"SIS_PGI_PMI_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05637","properties":[{"key":"EntryName","value":"SIS_PGI_PMI_2"},{"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":"2"}]},{"database":"InterPro","id":"IPR019490","properties":[{"key":"EntryName","value":"Glu6P/Mann6P_isomerase_C"}]},{"database":"InterPro","id":"IPR047640","properties":[{"key":"EntryName","value":"RpiR-like"}]},{"database":"InterPro","id":"IPR001347","properties":[{"key":"EntryName","value":"SIS_dom"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"InterPro","id":"IPR035484","properties":[{"key":"EntryName","value":"SIS_PGI/PMI_1"}]},{"database":"NCBIfam","id":"TIGR02128","properties":[{"key":"EntryName","value":"G6PI_arch"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006423","properties":[{"key":"EntryName","value":"PRK08674.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30514","properties":[{"key":"EntryName","value":"GLUCOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30514:SF10","properties":[{"key":"EntryName","value":"MURR_RPIR FAMILY TRANSCRIPTIONAL REGULATOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10432","properties":[{"key":"EntryName","value":"bact-PGI_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01380","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51464","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLTLIENFPKHLVDAMITAKKASFKQSNRAIKNVIITGLGGSGIGASMVQDLLSPHAEIPIIVNKDYHLPAFADENTLVIACSYSGETEETLAALAEAEEHSCEIAIITSGGTLLQMAKSKNYNYLQMPEGNPPRSMIGYSLVYQLYMLAYYGISRLALDNDIILSSNYLLEFREKIQSQARYIAVRLHKKIPAVYACSGFGSLAERFRQQLNENSKMLAWNGTVPEMNHNELVGWKGGDEHFAAIFIHTPFDDNRNAKRTEISSNIIQNFTSGVFHIHSEGETPLRAFFYLIHITDWISYYLSELNGVDVMDISAINQLKGELANFN","length":328,"molWeight":36665,"crc64":"E1B4F40DB6DD07D1","md5":"DA656C96A6BA9776557F40F7CEE680F4"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0004E6DB3E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZYJ0","uniProtkbId":"A0A368ZYJ0_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02102.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"ATP-dependent Clp protease proteolytic subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"3.4.21.92"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Endopeptidase Clp"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"clpP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02102.1"}],"value":"DES35_10573"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).","ecNumber":"3.4.21.92","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007039"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"Belongs to the peptidase S14 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02102.1"}],"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":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}]},{"type":"Active site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02102.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02102.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000005","properties":[{"key":"ProteinId","value":"RCX02102.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037359878.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000004.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZYJ0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0009368","properties":[{"key":"GoTerm","value":"C:endopeptidase Clp complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051117","properties":[{"key":"GoTerm","value":"F:ATPase binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07017","properties":[{"key":"EntryName","value":"S14_ClpP_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000002","properties":[{"key":"EntryName","value":"ATP-dependent Clp protease proteolytic subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00444","properties":[{"key":"EntryName","value":"ClpP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001907","properties":[{"key":"EntryName","value":"ClpP"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR023562","properties":[{"key":"EntryName","value":"ClpP/TepA"}]},{"database":"NCBIfam","id":"NF011091","properties":[{"key":"EntryName","value":"clpP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001368","properties":[{"key":"EntryName","value":"PRK00277.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009205","properties":[{"key":"EntryName","value":"PRK12553.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381:SF70","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00574","properties":[{"key":"EntryName","value":"CLP_protease"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00127","properties":[{"key":"EntryName","value":"CLPPROTEASEP"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDFGKEFKKYAIKHKSISSLNVESYLANSLTPYIIEERQLNVAQMDVFSRLMMDRIIFLGTAINDQVANIVQAQLLFLESVDPKKDIQIYLNSPGGSVYAGLGIYDTMQVVAPDVATICTGIAASMAAVLLCAGTKGKRTALKHSRIMIHQPMSGTQGQVSDMEIALKETLRVRDELYNILAQHTGQPFEKISADSDRDYWMRSEEAKEYGMIDDILLSKKTNANS","length":226,"molWeight":25163,"crc64":"4E51832C8BFC7FC6","md5":"EBE8772205747C2A51AC0E90AE72AD4E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":2},"uniParcId":"UPI0004E6C296"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZYK7","uniProtkbId":"A0A368ZYK7_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2018-11-07","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01206.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00559"}],"value":"Pyridoxine 5'-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"PNP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00559"}],"value":"2.6.99.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"pdxJ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01206.1"}],"value":"DES35_10719"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-amino-2-oxopropyl phosphate + 1-deoxy-D-xylulose 5-phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15265"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57279"},{"database":"ChEBI","id":"CHEBI:57792"},{"database":"ChEBI","id":"CHEBI:58589"}],"ecNumber":"2.6.99.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"Homooctamer; tetramer of dimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"Belongs to the PNP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01206.1"}],"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":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}]},{"type":"Active site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}]},{"type":"Active site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57279"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"3-amino-2-oxopropyl phosphate","id":"ChEBI:CHEBI:57279"}},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57279"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"3-amino-2-oxopropyl phosphate","id":"ChEBI:CHEBI:57279"}},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57279"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"3-amino-2-oxopropyl phosphate","id":"ChEBI:CHEBI:57279"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57279"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"ligand":{"name":"3-amino-2-oxopropyl phosphate","id":"ChEBI:CHEBI:57279"}},{"type":"Site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023096"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00279"}],"id":"KW-0664","category":"Biological process","name":"Pyridoxine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_00279"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01206.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01206.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000007","properties":[{"key":"ProteinId","value":"RCX01206.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_051889300.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000003.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZYK7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00244","properties":[{"key":"RectionId","value":"UER00313"}]},{"database":"Proteomes","id":"UP000253517","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:0033856","properties":[{"key":"GoTerm","value":"F:pyridoxine 5'-phosphate synthase activity"},{"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":"CDD","id":"cd00003","properties":[{"key":"EntryName","value":"PNPsynthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000150","properties":[{"key":"EntryName","value":"Pyridoxine 5'-phosphate synthase"},{"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_00279","properties":[{"key":"EntryName","value":"PdxJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR004569","properties":[{"key":"EntryName","value":"PyrdxlP_synth_PdxJ"}]},{"database":"InterPro","id":"IPR036130","properties":[{"key":"EntryName","value":"Pyridoxine-5'_phos_synth"}]},{"database":"NCBIfam","id":"TIGR00559","properties":[{"key":"EntryName","value":"pdxJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003625","properties":[{"key":"EntryName","value":"PRK05265.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003626","properties":[{"key":"EntryName","value":"PRK05265.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30456","properties":[{"key":"EntryName","value":"PYRIDOXINE 5'-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30456:SF0","properties":[{"key":"EntryName","value":"PYRIDOXINE 5'-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03740","properties":[{"key":"EntryName","value":"PdxJ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63892","properties":[{"key":"EntryName","value":"Pyridoxine 5'-phosphate synthase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKTKLSVNINKIATLRNSRGGNVPDVLQAAIDCQRFGAEGITVHPRPDERHIRYSDVRAIRPIITTEFNIEGYPSEKFLQLVEEVRPHQVTLVPDPPDALTSNAGWDTQAHLDFLKEVIARIKATGARVSLFVETNEEDIKGAALAGADRIELYTEDYARGYNKDPENAVAPYAVCAAIAHSLGLGVNAGHDLNLDNLRYFVAQVPHLLEVSIGHALISDALYYGLENTIQMYLRQIALGHQDKQAQSSESTSVAD","length":257,"molWeight":28314,"crc64":"AE17C07FDE0C4AC8","md5":"19D91B10943961FC44F66551F1CDA862"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":3,"Binding site":7,"Site":1},"uniParcId":"UPI0004E717FF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZYP4","uniProtkbId":"A0A368ZYP4_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":26,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02071.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Octanoyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"2.3.1.181"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Lipoate-protein ligase B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Lipoyl/octanoyl transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"lipB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02071.1"}],"value":"DES35_10542"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024732"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octanoyl-[ACP] + L-lysyl-[protein] = N(6)-octanoyl-L-lysyl-[protein] + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17665"},{"database":"Rhea","id":"RHEA-COMP:9636"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:9928"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78463"},{"database":"ChEBI","id":"CHEBI:78809"}],"ecNumber":"2.3.1.181","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004821"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Belongs to the LipB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02071.1"}],"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":49,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"BPL/LPL catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51733"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-1"}]},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"Lowers pKa of active site Cys","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_00013"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02071.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02071.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000005","properties":[{"key":"ProteinId","value":"RCX02071.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366481.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000004.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZYP4","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00538","properties":[{"key":"RectionId","value":"UER00592"}]},{"database":"Proteomes","id":"UP000253517","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:0033819","properties":[{"key":"GoTerm","value":"F:lipoyl(octanoyl) transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009249","properties":[{"key":"GoTerm","value":"P:protein lipoylation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16444","properties":[{"key":"EntryName","value":"LipB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.930.10:FF:000035","properties":[{"key":"EntryName","value":"Putative lipoyltransferase 2, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00013","properties":[{"key":"EntryName","value":"LipB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR004143","properties":[{"key":"EntryName","value":"BPL_LPL_catalytic"}]},{"database":"InterPro","id":"IPR000544","properties":[{"key":"EntryName","value":"Octanoyltransferase"}]},{"database":"InterPro","id":"IPR020605","properties":[{"key":"EntryName","value":"Octanoyltransferase_CS"}]},{"database":"NCBIfam","id":"NF010925","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00214","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10993","properties":[{"key":"EntryName","value":"OCTANOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10993:SF12","properties":[{"key":"EntryName","value":"OCTANOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21948","properties":[{"key":"EntryName","value":"LplA-B_cat"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016262","properties":[{"key":"EntryName","value":"LPLase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51733","properties":[{"key":"EntryName","value":"BPL_LPL_CATALYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01313","properties":[{"key":"EntryName","value":"LIPB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTELQSTRRKVKILRRGLTEYATAWAEQEALFKVVEQGKLLRRKGQTDFFPVNYLITVEHPPVYTLGKSANSGNLIYPEEFYTSKGAQIFHINRGGDVTFHGHGQLVVYPIFDLDQFFTDIHRYLRYLEEAVINTLADYGVQGERSPGETGVWLDPKGKNPRKICAMGVRAARWITMHGLALNVNTDLSWFDYIIPCGIKGKSVTSMAKETNQYIPLTEIEEKLLKHLKNLFEFEEISD","length":239,"molWeight":27376,"crc64":"0D6D12A51914477A","md5":"2B323FBC5C01C56B0920DFDD5DF89B8D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":3,"Site":1},"uniParcId":"UPI000DF41673"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZYQ1","uniProtkbId":"A0A368ZYQ1_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02150.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Energy-dependent translational throttle protein EttA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"3.6.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Translational regulatory factor EttA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"ettA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02150.1"}],"value":"DES35_105122"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Monomer. Probably contacts ribosomal proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P-site containing tRNA(fMet)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Associates with ribosomes and polysomes"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"The P-site tRNA interaction motif (PtIM domain) probably interacts with the P-site tRNA(fMet) as well as the 23S rRNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"The arm domain is inserted in the first ABC transporter domain. Probably contacts ribosomal protein L1"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005868"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Belongs to the ABC transporter superfamily. ABCF family. Translational throttle EttA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02150.1"}],"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":1,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"ABC transporter","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50893"}]},{"type":"Domain","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"ABC transporter","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50893"}]},{"type":"Region","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"PtIM","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}]},{"type":"Coiled coil","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"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_00847"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022730"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022845"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0810","category":"Biological process","name":"Translation regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00847"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02150.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02150.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000005","properties":[{"key":"ProteinId","value":"RCX02150.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A368ZYQ1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043022","properties":[{"key":"GoTerm","value":"F:ribosome binding"},{"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:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0045900","properties":[{"key":"GoTerm","value":"P:negative regulation of translational elongation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03221","properties":[{"key":"EntryName","value":"ABCF_EF-3"},{"key":"MatchStatus","value":"2"}]},{"database":"FunFam","id":"3.40.50.300:FF:000183","properties":[{"key":"EntryName","value":"ABC transporter ATP-binding protein yjjK"},{"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":"HAMAP","id":"MF_00847","properties":[{"key":"EntryName","value":"EttA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR032781","properties":[{"key":"EntryName","value":"ABC_tran_Xtn"}]},{"database":"InterPro","id":"IPR003439","properties":[{"key":"EntryName","value":"ABC_transporter-like_ATP-bd"}]},{"database":"InterPro","id":"IPR017871","properties":[{"key":"EntryName","value":"ABC_transporter-like_CS"}]},{"database":"InterPro","id":"IPR022374","properties":[{"key":"EntryName","value":"EttA"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR03719","properties":[{"key":"EntryName","value":"ABC_ABC_ChvD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008775","properties":[{"key":"EntryName","value":"ettA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43858:SF1","properties":[{"key":"EntryName","value":"ABC TRANSPORTER-RELATED PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43858","properties":[{"key":"EntryName","value":"ENERGY-DEPENDENT TRANSLATIONAL THROTTLE PROTEIN ETTA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00005","properties":[{"key":"EntryName","value":"ABC_tran"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF12848","properties":[{"key":"EntryName","value":"ABC_tran_Xtn"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00211","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50893","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSGVTKTYSSTNKTVLKDIYLSFFYGAKIGILGLNGSGKSTLLKIIAGVDKNYQGNVVWSPGYTVGYLEQEPQLDPNKTVIEVVREGVSDVMALLDEYNTINDQFGLPEVYENPEKMDKLMARQAELQDKIEALGAWEIDTKLERAMDALQCPDPDKPISVLSGGEKRRVALCRLLLKQPDVLLLDEPTNHLDAESVLWLEHHLQQYPGTVLAVTHDRYFLDNVAGWILELDRGEGIPWKGNYSSWLEQKTKRLEQEEKQASKRRKTLERELEWVKMNPKGRQAKSKARLANYEKMLNEEQKEKEEKLEIYIPPGPRLGTQVIEARHVAKAYGDKLLYEDLNFNLPPAGIVGIIGPNGAGKTTIFRMIMGLEKPDAGEFIIGDTVKISYVDQSHEKMHPDKTIFEIIADGQEEFELGGRRINTRAYLGRFNFSGSDQNKKVGMLSGGERNRLHLAMALKEGGNVLLLDEPTNDLDVNTLRALEEALENFAGCAVIISHDRWFMDRVCTHILAFEGDAKVYYFEGSFSEYEENKRKRLGETTPKRFRYKKLVKEG","length":554,"molWeight":62825,"crc64":"2AB941BC662E22AE","md5":"5828929011F5BAC923D05802CACDAF37"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":2,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Coiled coil":1,"Binding site":3},"uniParcId":"UPI000AAE36BF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZ44","uniProtkbId":"A0A368ZZ44_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01097.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00040883"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Type III pantothenate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012102"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"2.7.1.33"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"PanK-III"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Pantothenic acid kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"coaX"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01097.1"}],"value":"DES35_1082"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16373"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29032"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.33","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001206"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001958"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"NH4(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:28938"}},{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"A monovalent cation. Ammonium or potassium."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005225"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038036"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Belongs to the type III pantothenate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01097.1"}],"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":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022993"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"id":"KW-0173","category":"Biological process","name":"Coenzyme A biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01274"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_01274"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01097.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX01097.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000008","properties":[{"key":"ProteinId","value":"RCX01097.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037361059.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000002.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZ44","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00352"}]},{"database":"Proteomes","id":"UP000253517","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:0004594","properties":[{"key":"GoTerm","value":"F:pantothenate kinase 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":"CDD","id":"cd24015","properties":[{"key":"EntryName","value":"ASKHA_NBD_PanK-III"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01274","properties":[{"key":"EntryName","value":"Pantothen_kinase_3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR004619","properties":[{"key":"EntryName","value":"Type_III_PanK"}]},{"database":"NCBIfam","id":"TIGR00671","properties":[{"key":"EntryName","value":"baf"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34265","properties":[{"key":"EntryName","value":"TYPE III PANTOTHENATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34265:SF1","properties":[{"key":"EntryName","value":"TYPE III PANTOTHENATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03309","properties":[{"key":"EntryName","value":"Pan_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MKKYLLADVGNTFTKIRIYENSEYQFLTFPTIKPDGNPDGKQLQDLVSANQIDDVLYSTVVPEWHRIFNNLEVKGVVRKVSVQMKLPFEMKYQTPETLGSDRIALLAAAAEAGFHHHCTLIVSAGTCITFDILHERTYLGGAISPGLAMRAKAMNHFTKALPLVTVNLIDIPVNGQLFIGQDTAQCLWAGSVQSAALEIDQYIDRLKSKFSKLKIYLTGGDANTLEKMIKSDIFARPNMCLDGLNILYKLNA","length":252,"molWeight":28057,"crc64":"2F147C1285A7C17E","md5":"DF6FAA5A16D1B761F7764458571FB360"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":1,"Binding site":5},"uniParcId":"UPI0004E7061A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZ82","uniProtkbId":"A0A368ZZ82_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-11-07","entryVersion":26,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02330.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Lipoprotein signal peptidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"3.4.23.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Prolipoprotein signal peptidase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Signal peptidase II"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"SPase II"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"lspA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02330.1"}],"value":"DES35_10490"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"This protein specifically catalyzes the removal of signal peptides from prolipoproteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.","ecNumber":"3.4.23.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Protein modification; lipoprotein biosynthesis (signal peptide cleavage)"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006139"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004181"}],"value":"Belongs to the peptidase A8 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02330.1"}],"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":61,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Transmembrane","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Transmembrane","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Active site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Active site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022750"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0064","category":"Molecular function","name":"Aspartyl protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_00161"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02330.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02330.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02330.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037358928.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000005.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZ82","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00665","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0004190","properties":[{"key":"GoTerm","value":"F:aspartic-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"HAMAP","id":"MF_00161","properties":[{"key":"EntryName","value":"LspA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001872","properties":[{"key":"EntryName","value":"Peptidase_A8"}]},{"database":"NCBIfam","id":"NF011369","properties":[{"key":"EntryName","value":"PRK14788.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33695","properties":[{"key":"EntryName","value":"LIPOPROTEIN SIGNAL PEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33695:SF1","properties":[{"key":"EntryName","value":"LIPOPROTEIN SIGNAL PEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01252","properties":[{"key":"EntryName","value":"Peptidase_A8"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00781","properties":[{"key":"EntryName","value":"LIPOSIGPTASE"}]}],"sequence":{"value":"MRQNLLIVALILLADQALKIWVKLTMMLGQEHRITDWFILHFTENPGMAFGLEWGGDVGKYLLTIFRIAASVWIFTWLVKLNRNHVPAVAQISVALVLAGAVGNLIDSLFYGLLFDHSYHQVATLFPKGGGYAGFMLGHVVDMFYFPLIHTTLPDWIPFWGGKEFLFFQPIFNIADASITVGVGLMIVYQRYLFEKNAQQHSVA","length":204,"molWeight":23076,"crc64":"170DF9E891D001B3","md5":"F2760A15BD949DEE23BE83ADF38DB568"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Transmembrane":3,"Active site":2},"uniParcId":"UPI0004E6FDC1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZA5","uniProtkbId":"A0A368ZZA5_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033765"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"2.8.4.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00080698"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"tRNA-i(6)A37 methylthiotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"miaB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02285.1"}],"value":"DES35_10444"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003234"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-dimethylallyladenosine(37) in tRNA + (sulfur carrier)-SH + AH2 + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + (sulfur carrier)-H + 5'-deoxyadenosine + L-methionine + A + S-adenosyl-L-homocysteine + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:37067"},{"database":"Rhea","id":"RHEA-COMP:10375"},{"database":"Rhea","id":"RHEA-COMP:10376"},{"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:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64428"},{"database":"ChEBI","id":"CHEBI:74415"},{"database":"ChEBI","id":"CHEBI:74417"}],"ecNumber":"2.8.4.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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_01864"},{"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."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00780"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"value":"Belongs to the methylthiotransferase family. MiaB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02285.1"}],"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":26,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"MTTase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51449"}]},{"type":"Domain","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Domain","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"TRAM","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50926"}]},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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":180,"modifier":"EXACT"},"end":{"value":180,"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":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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":184,"modifier":"EXACT"},"end":{"value":184,"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":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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":187,"modifier":"EXACT"},"end":{"value":187,"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":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"},{"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_01864"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"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_01864"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01864"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02285.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366395.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000006.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZA5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0035597","properties":[{"key":"GoTerm","value":"F:tRNA-2-methylthio-N(6)-dimethylallyladenosine(37) synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.12160:FF:000003","properties":[{"key":"EntryName","value":"CDK5 regulatory subunit-associated protein 1"},{"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":"3.80.30.20","properties":[{"key":"EntryName","value":"tm_1862 like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01864","properties":[{"key":"EntryName","value":"tRNA_metthiotr_MiaB"},{"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":"IPR006463","properties":[{"key":"EntryName","value":"MiaB_methiolase"}]},{"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":"TIGR01574","properties":[{"key":"EntryName","value":"miaB-methiolase"},{"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":"PTHR43020","properties":[{"key":"EntryName","value":"CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43020:SF2","properties":[{"key":"EntryName","value":"MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01938","properties":[{"key":"EntryName","value":"TRAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00919","properties":[{"key":"EntryName","value":"UPF0004"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00273","properties":[{"key":"EntryName","value":"(dimethylallyl)adenosine_tRNA"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01082","properties":[{"key":"EntryName","value":"B12-binding_domain_containing"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00413","properties":[{"key":"EntryName","value":"CDK5RAP1"},{"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":"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":"MHHYGNKIIDESRQGEALMLESEGHKKLYIESYGCQMNFSDSEIVASILAGEGYSTTKNPEDADLVLLNTCSIREKAEQTVRNRLSHLQYLKKTKPAVKIGVLGCMAERIKDKLLDEEKLVDLVVGPDAYRDLPELLKEVNDGRKAVNVILSKEETYGDINPVRLGGNGISAFISIMRGCDNMCTFCVVPFTRGRERSRNPQSIIEEAVQLQDAGYKEITLLGQNVDSYLWYGGGLKKDFAKASEIARASAVRFAELLRRVAEAVPGMRIRFSTSNPQDMTEDVLYTIAEYPNICKYIHLPVQSGSSRILKAMNRGHTREQYMELIEKIRSIIPDCGLSHDMIAGFPGETEEDHQDTLSLMEFVKYDFGYMFKYSERPGTYAARHLRDDVPDEVKTRRLNEIIDLQQKHSLYRNQQHLGKTVEVLVEGTSRKSEDHWFGRTTQNTVVVFPKEQAKPGDRVWVTVEYCTSATLLGKLASLSC","length":481,"molWeight":54411,"crc64":"E06D8121889097E3","md5":"BFA86FE927CC809DC2079167580CE8E8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Binding site":9},"uniParcId":"UPI000DF1C38C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZB6","uniProtkbId":"A0A368ZZB6_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02249.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029504"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"value":"UvrABC system protein B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"value":"Protein UvrB"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"value":"Excinuclease ABC subunit B"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"value":"uvrB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02249.1"}],"value":"DES35_1048"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"value":"The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026033"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003587"}],"value":"Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003587"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"value":"The beta-hairpin motif is involved in DNA binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003587"}],"value":"Belongs to the UvrB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02249.1"}],"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":160,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":591,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Domain","location":{"start":{"value":628,"modifier":"EXACT"},"end":{"value":663,"modifier":"EXACT"}},"description":"UVR","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50151"}]},{"type":"Coiled coil","location":{"start":{"value":631,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Motif","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"Beta-hairpin","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}]},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"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":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022769"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0228","category":"Biological process","name":"DNA excision"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022881"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0267","category":"Molecular function","name":"Excision nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023236"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00204"}],"id":"KW-0742","category":"Biological process","name":"SOS response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02249.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02249.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02249.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366374.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000006.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZB6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0009380","properties":[{"key":"GoTerm","value":"C:excinuclease repair complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009381","properties":[{"key":"GoTerm","value":"F:excinuclease ABC activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006289","properties":[{"key":"GoTerm","value":"P:nucleotide-excision repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009432","properties":[{"key":"GoTerm","value":"P:SOS response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd17916","properties":[{"key":"EntryName","value":"DEXHc_UvrB"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18790","properties":[{"key":"EntryName","value":"SF2_C_UvrB"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"4.10.860.10","properties":[{"key":"EntryName","value":"UVR domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00204","properties":[{"key":"EntryName","value":"UvrB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006935","properties":[{"key":"EntryName","value":"Helicase/UvrB_N"}]},{"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":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR001943","properties":[{"key":"EntryName","value":"UVR_dom"}]},{"database":"InterPro","id":"IPR036876","properties":[{"key":"EntryName","value":"UVR_dom_sf"}]},{"database":"InterPro","id":"IPR004807","properties":[{"key":"EntryName","value":"UvrB"}]},{"database":"InterPro","id":"IPR060262","properties":[{"key":"EntryName","value":"UvrB_3rd"}]},{"database":"InterPro","id":"IPR041471","properties":[{"key":"EntryName","value":"UvrB_inter"}]},{"database":"InterPro","id":"IPR024759","properties":[{"key":"EntryName","value":"UvrB_YAD/RRR_dom"}]},{"database":"NCBIfam","id":"NF003673","properties":[{"key":"EntryName","value":"uvrB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00631","properties":[{"key":"EntryName","value":"uvrb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24029","properties":[{"key":"EntryName","value":"UVRABC SYSTEM PROTEIN B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24029:SF0","properties":[{"key":"EntryName","value":"UVRABC SYSTEM PROTEIN B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04851","properties":[{"key":"EntryName","value":"ResIII"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02151","properties":[{"key":"EntryName","value":"UVR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12344","properties":[{"key":"EntryName","value":"UvrB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF27431","properties":[{"key":"EntryName","value":"UvrB_3rd"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17757","properties":[{"key":"EntryName","value":"UvrB_inter"},{"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":"SUPFAM","id":"SSF46600","properties":[{"key":"EntryName","value":"C-terminal UvrC-binding domain of UvrB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"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":"PS50151","properties":[{"key":"EntryName","value":"UVR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEFKLEAPYKPTGDQPEAIRQLVSGLKNGERAQTLLGVTGSGKTFTMANVVEQIQRPTLVLSHNKTLAAQLYGEFKQFFPNNAVEYFVSYYDYYQPEAYIPSTNTYIEKDLSINDEIEKLRLSTTSALLSGRRDVLVVASVSCLYGIGNPEEFSKGVIELYKGQVIARTKLLHQFVSSLYSRTSHEFARGRFRVKGDVVDIFPAYSDYAVRIHFWGNEIELLEEVDPVTGAILSEFERVRIYPANIFMTSPVRLQEAIRQIQHDLVKQVDFFLKQGKPLEAKRLEERTNFDLEMIKELGYCSGIENYSRYLDGRAPGTRPFCLIDYFPKDWLLIVDESHVTIPQVRAMYGGDRSRKETLVEYGFRLPAALDNRPLRFEEFESLINQVIYVSATPGDYELQASGGVIVEQLIRPTGMLDPIVEVRPTTNQIDDLMDEIQKRVELDERVLVTTLTKRMAEELYKYFSRFGVRCRYIHSDVDTLERVEILRDLRMGLFDVLIGVNLLREGLDLPEVSLVAILDADKEGFLRNERSLVQTIGRAARHPNGMAILYANTITDSMQRTIDETNRRRAVQSEYNSKHGITPKILQKSLDTHLPVASRQNLAAEPMENFLISEPETPYLQSPETLKKQIEKTRKEMEQAAKALDFIKAAQLRDQMLSLEAKYKELYSL","length":670,"molWeight":76746,"crc64":"43C86E824D3CD9E3","md5":"D67B75A8E4BE876882A76B113259BFC2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Coiled coil":1,"Motif":1,"Binding site":1},"uniParcId":"UPI000DF359BE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZC5","uniProtkbId":"A0A368ZZC5_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02259.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Fused isobutyryl-CoA mutase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Isobutyryl-CoA mutase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"ICM"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"5.4.99.13"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"P-loop GTPase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"3.6.5.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"G-protein chaperone"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"icmF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02259.1"}],"value":"DES35_10418"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA = butanoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13141"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57371"}],"ecNumber":"5.4.99.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"adenosylcob(III)alamin","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001922"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18408"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Is composed of four functional domains: the N-terminal 5'-deoxyadenosylcobalamin binding region that is homologous to the small subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely acts as a chaperone for ICM, a structured linker region involved in dimer formation, and a C-terminal part that is homologous to the large substrate-binding subunit of ICM (IcmA)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Belongs to the IcmF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02259.1"}],"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":36,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"B12-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51332"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"},{"database":"ChEBI","id":"CHEBI:27638"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"},"ligandPart":{"name":"Co","id":"ChEBI:CHEBI:27638"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":602,"modifier":"EXACT"},"end":{"value":602,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":637,"modifier":"EXACT"},"end":{"value":637,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":787,"modifier":"EXACT"},"end":{"value":787,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":831,"modifier":"EXACT"},"end":{"value":831,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":880,"modifier":"EXACT"},"end":{"value":880,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":915,"modifier":"EXACT"},"end":{"value":915,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":920,"modifier":"EXACT"},"end":{"value":920,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":1032,"modifier":"EXACT"},"end":{"value":1032,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":1151,"modifier":"EXACT"},"end":{"value":1151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0846","category":"Ligand","name":"Cobalamin"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02259.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02259.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02259.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A368ZZC5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031419","properties":[{"key":"GoTerm","value":"F:cobalamin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0047727","properties":[{"key":"GoTerm","value":"F:isobutyryl-CoA mutase 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:0034784","properties":[{"key":"GoTerm","value":"F:pivalyl-CoA mutase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006637","properties":[{"key":"GoTerm","value":"P:acyl-CoA metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02071","properties":[{"key":"EntryName","value":"MM_CoA_mut_B12_BD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.280","properties":[{"key":"EntryName","value":"Cobalamin-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.240","properties":[{"key":"EntryName","value":"Methylmalonyl-CoA mutase"},{"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_02050","properties":[{"key":"EntryName","value":"IcmF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016176","properties":[{"key":"EntryName","value":"Cbl-dep_enz_cat"}]},{"database":"InterPro","id":"IPR006158","properties":[{"key":"EntryName","value":"Cobalamin-bd"}]},{"database":"InterPro","id":"IPR036724","properties":[{"key":"EntryName","value":"Cobalamin-bd_sf"}]},{"database":"InterPro","id":"IPR052040","properties":[{"key":"EntryName","value":"GTPase/Isobutyryl-CoA_mutase"}]},{"database":"InterPro","id":"IPR033669","properties":[{"key":"EntryName","value":"IcmF"}]},{"database":"InterPro","id":"IPR006099","properties":[{"key":"EntryName","value":"MeMalonylCoA_mutase_a/b_cat"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"PANTHER","id":"PTHR43087:SF1","properties":[{"key":"EntryName","value":"LAO_AO TRANSPORT SYSTEM ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43087","properties":[{"key":"EntryName","value":"LYSINE/ARGININE/ORNITHINE TRANSPORT SYSTEM KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02310","properties":[{"key":"EntryName","value":"B12-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03308","properties":[{"key":"EntryName","value":"MeaB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01642","properties":[{"key":"EntryName","value":"MM_CoA_mutase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52242","properties":[{"key":"EntryName","value":"Cobalamin (vitamin B12)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51703","properties":[{"key":"EntryName","value":"Cobalamin (vitamin B12)-dependent enzymes"},{"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":"PS51332","properties":[{"key":"EntryName","value":"B12_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYPIHNIAQRTPIFAHDSEELNDMSETATPYKPKNKVRIVTAASLFDGHDAAINIMRRIMQATGCEVIHLGHDRSVEEIVNCAIQEDAQAIAITSYQGGHMEFFKYMYDLLKEKGASHIKIFGGGGGTILPTEIQELHNYGITRIYHPDDGRAMGLQGMINDVVMKADFPIGYPLNGQIKKLGNKPENWTAIARLISAAENFPDESRAELEAIKNLAEESHTPVLGITGTGGAGKSSLVDELVRRFILDFPDKTIGIISVDPSKRKTGGALLGDRIRMNSIHHPRVYMRSLATRQSNLALSRYVGDAISVLKAANYDLIILETSGIGQSDTEILDYSDVSLYVMTPEYGAATQLEKIDMLDFADLIALNKFDKRGAADALRDVKKQYQRNHQLWSKPLDEMPVYGTIASQFNDPGMNRLYKAVMDTITAKTGANLKSNFAATDEMSEKIYIIPPQRTRYLSEITENNRKYNKWVEQQAEIAQKLYNIHSTIEHLTNTDLNYKDELIAQLKNEFDKVKLDLDPHNWQLIEKFDDKAQKYRNDEYIFTVRDKEIRIKTYTESLSHLKIPKIATPRYKAWGDLLRWLLQENFPGEFPYTAGIYPFKRTGEDPTRMFAGEGSPERTNKRFHYLSLGMPAARLSTAFDSVTLYGRNPDLRPDIYGKIGNSGVSVCCLDDAKKLYSGFNLAAPTTSVSMTINGPAPMLLAFFMNTAIDQQCELYIRQHGLEHLVEQKLKELYDDRDLPRPGYNAPLPEGNDGLGLLLLGITGDQILEQETYNRIKEDTLGVVRGTVQADILKEDQAQNTCIFSTEFALRLMGDVQQYFIDHRVRNFYSVSISGYHIAEAGANPITQLAFTLANGFTYVEYYLSRGMDINDFGPNLSFFFSNGIDPEYAVIGRAARRIWAKAMKYKYGAYPRAQMLKYHIQTSGRSLHAQEIDFNDIRTTLQALYAIYDNCNSLHTNAYDEAITTPTEESVRRAVAIQLIINKELGLAKNENPLQGSFIIEELTDLVEEAVMLEFDRITERGGVLGAMETMYQRSKIQEESLYYETLKHTGELPIIGVNTFLSSKGSPTIIPAEVIRATEEEKQQQVETVRRLHTFRPDKSTQMLRAIQEAAIRNENIFAVLMEASKYCTLGQMTEAMFQVGGQYRRNM","length":1152,"molWeight":130138,"crc64":"20D921F7E01570E5","md5":"B0798E28C5FF3B401ED019804290E68F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":21},"uniParcId":"UPI000DFEA520"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZD2","uniProtkbId":"A0A368ZZD2_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02269.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"value":"Succinate--CoA ligase [ADP-forming] subunit alpha"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"value":"6.2.1.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"value":"Succinyl-CoA synthetase subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"value":"SCS-alpha"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"value":"sucD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02269.1"}],"value":"DES35_10428"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000699"}],"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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta 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_01988"}]}},{"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_01988"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000699"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005064"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000699"}],"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_01988"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000699"}],"value":"Heterotetramer of two alpha and two beta subunits"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000677"}],"value":"Belongs to the succinate/malate CoA ligase alpha subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02269.1"}],"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":4,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"CoA-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00881"}]},{"type":"Active site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Tele-phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001553-1"}]},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"ligand":{"name":"substrate","note":"ligand shared with subunit beta"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01988"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_01988"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02269.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02269.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02269.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037360506.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000006.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZD2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00223","properties":[{"key":"RectionId","value":"UER00999"}]},{"database":"Proteomes","id":"UP000253517","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009361","properties":[{"key":"GoTerm","value":"C:succinate-CoA ligase complex (ADP-forming)"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:0004776","properties":[{"key":"GoTerm","value":"F:succinate-CoA ligase (GDP-forming) activity"},{"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":"3.40.50.261:FF:000006","properties":[{"key":"EntryName","value":"Succinate--CoA ligase [ADP-forming] subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000002","properties":[{"key":"EntryName","value":"Succinate--CoA ligase [ADP-forming] subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.261","properties":[{"key":"EntryName","value":"Succinyl-CoA synthetase domains"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01988","properties":[{"key":"EntryName","value":"Succ_CoA_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017440","properties":[{"key":"EntryName","value":"Cit_synth/succinyl-CoA_lig_AS"}]},{"database":"InterPro","id":"IPR033847","properties":[{"key":"EntryName","value":"Citrt_syn/SCS-alpha_CS"}]},{"database":"InterPro","id":"IPR003781","properties":[{"key":"EntryName","value":"CoA-bd"}]},{"database":"InterPro","id":"IPR005810","properties":[{"key":"EntryName","value":"CoA_lig_alpha"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR005811","properties":[{"key":"EntryName","value":"SUCC_ACL_C"}]},{"database":"InterPro","id":"IPR016102","properties":[{"key":"EntryName","value":"Succinyl-CoA_synth-like"}]},{"database":"NCBIfam","id":"TIGR01019","properties":[{"key":"EntryName","value":"sucCoAalpha"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004230","properties":[{"key":"EntryName","value":"sucD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11117:SF2","properties":[{"key":"EntryName","value":"SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11117","properties":[{"key":"EntryName","value":"SUCCINYL-COA LIGASE SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02629","properties":[{"key":"EntryName","value":"CoA_binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00549","properties":[{"key":"EntryName","value":"Ligase_CoA"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001553","properties":[{"key":"EntryName","value":"SucCS_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01798","properties":[{"key":"EntryName","value":"SCOASYNTHASE"}]},{"database":"SMART","id":"SM00881","properties":[{"key":"EntryName","value":"CoA_binding"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52210","properties":[{"key":"EntryName","value":"Succinyl-CoA synthetase domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01216","properties":[{"key":"EntryName","value":"SUCCINYL_COA_LIG_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00399","properties":[{"key":"EntryName","value":"SUCCINYL_COA_LIG_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVLVNKHSRVIVQGFTGKEGTFHASQMIEYGTQVVGGVTPGKGGTKHLDRPVFNTVEQAVKETGADVSIIFVPPAFAADSIMEAAEAGIQVIVAITEGIPVRDMVVAKNYLKTKETVLIGPNCPGVITAEEAKVGIMPGFVFKKGSIGIVSKSGTLTYEAADQIVKAGLGITTAIGIGGDPIIGTPTREAIKMLMDDPETQGIVMIGEIGGNYEALAAEWIQENGTKPVVGFIAGETAPKGRTMGHAGAIVGGKDDTAQAKKAIMRQCGIHVVDSPAEIGKKMAEVISGL","length":291,"molWeight":30182,"crc64":"CF0799373EF48AB0","md5":"396197582AF988A8373E0C1E6AA40BEA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":4},"uniParcId":"UPI0004E79F38"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZE1","uniProtkbId":"A0A368ZZE1_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-11-07","entryVersion":26,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine hydroxymethyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"SHMT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"2.1.2.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02321.1"}],"value":"DES35_10481"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02321.1"}],"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":3,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Plays an important role in substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]},{"type":"Modified residue","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02321.1"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02321.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037361247.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000006.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZE1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00193","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00288","properties":[{"key":"RectionId","value":"UER01023"}]},{"database":"Proteomes","id":"UP000253517","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:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase 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:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"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_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MWKDDYLFDLIKKEKRRQTDGVELIASENFASEQVMKAMGSVLTNKYAEGFPGRRYYGGCEVVDEVETEAINRAKLLFGAQYACVQPHSGSQANAAVYLALLKPGDKIMGFDLSHGGHLTHGSPVSFSGKLYQAAFYGVEKETGLIDYENVRKRVLEEKPKLLICGASAYSRDINYAKFREIADEAGAFLLADISHPSGLIAKGVLNDPLPHCHFVTTTTHKTLRGPRGGLILMGNDFENPFGLKTPKGEIRMMSSLIDAAVFPGVQGGPLEHIIAAKAVAFGEALTDNFMAYILQVQKNARAMAGALLDMNYQIISGGTDNHLMLIDLRNKNITGKAAETALGKAGITVNKNMVPFDDKSPFVTSGIRIGTPAITTRGLDEKDCIQLAYWINEAIIHHDKDNQLAKIQKEVKKFMKQFPLFHWHKI","length":427,"molWeight":47065,"crc64":"0631A0FFC889F9E7","md5":"11D84FAD02F6065EAB371B91899097A7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI0004E699F6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZG9","uniProtkbId":"A0A368ZZG9_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Nucleoside diphosphate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"NDK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"NDP kinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"2.7.4.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Nucleoside-2-P kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"ndk"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02422.1"}],"value":"DES35_104183"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44640"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:73316"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.6","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18113"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57930"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.6","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008142"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004011"}],"value":"Belongs to the NDK family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02422.1"}],"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":3,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Nucleoside diphosphate kinase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00562"}]},{"type":"Active site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Pros-phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"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_00451"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02422.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037359114.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000005.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZG9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000253517","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:0016020","properties":[{"key":"GoTerm","value":"C: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:0004550","properties":[{"key":"GoTerm","value":"F:nucleoside diphosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006241","properties":[{"key":"GoTerm","value":"P:CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006183","properties":[{"key":"GoTerm","value":"P:GTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04413","properties":[{"key":"EntryName","value":"NDPk_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.141:FF:000017","properties":[{"key":"EntryName","value":"Nucleoside diphosphate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.141","properties":[{"key":"EntryName","value":"Nucleoside diphosphate kinase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00451","properties":[{"key":"EntryName","value":"NDP_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR034907","properties":[{"key":"EntryName","value":"NDK-like_dom"}]},{"database":"InterPro","id":"IPR036850","properties":[{"key":"EntryName","value":"NDK-like_dom_sf"}]},{"database":"InterPro","id":"IPR001564","properties":[{"key":"EntryName","value":"Nucleoside_diP_kinase"}]},{"database":"NCBIfam","id":"NF001908","properties":[{"key":"EntryName","value":"ndk"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011116","properties":[{"key":"EntryName","value":"PRK14545.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46161","properties":[{"key":"EntryName","value":"NUCLEOSIDE DIPHOSPHATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46161:SF3","properties":[{"key":"EntryName","value":"NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00334","properties":[{"key":"EntryName","value":"NDK"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01243","properties":[{"key":"EntryName","value":"NUCDPKINASE"}]},{"database":"SMART","id":"SM00562","properties":[{"key":"EntryName","value":"NDK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54919","properties":[{"key":"EntryName","value":"Nucleoside diphosphate kinase, NDK"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51374","properties":[{"key":"EntryName","value":"NDPK_LIKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRRITFTMIKPDAVADGNTGAILNRIEGAGFRIVAMKKTQLSKAEAEKFYGIHKDRPFFGELVEYMTSGPIVAAILEKENAVEDFRKLIGATDPAKAEEGTIRKMFAKSIAANAIHGSDSDENAVIESNFFFSERERY","length":139,"molWeight":15467,"crc64":"87E852F35136561A","md5":"EE33DCC56D5E28C5CEC55D83CB407FA9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":6},"uniParcId":"UPI0004E7A227"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A368ZZJ2","uniProtkbId":"A0A368ZZJ2_9FLAO","entryAudit":{"firstPublicDate":"2018-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-11-07","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Schleiferia thermophila","taxonId":884107,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02353.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Schleiferiaceae","Schleiferia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Diaminopimelate epimerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"DAP epimerase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"5.1.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"PLP-independent amino acid racemase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"dapF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02353.1"}],"value":"DES35_104113"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Catalyzes the stereoinversion of LL-2,6-diaminopimelate (L,L-DAP) to meso-diaminopimelate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S,6S)-2,6-diaminopimelate = meso-2,6-diaminopimelate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15393"},{"database":"ChEBI","id":"CHEBI:57609"},{"database":"ChEBI","id":"CHEBI:57791"}],"ecNumber":"5.1.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Belongs to the diaminopimelate epimerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02353.1"}],"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":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}]},{"type":"Active site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Could be important to modulate the pK values of the two catalytic cysteine residues","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}]},{"type":"Site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Could be important to modulate the pK values of the two catalytic cysteine residues","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00197"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-10F208IJOS4PL","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the most valuable type-strain genomes for metagenomic binning, comparative biology and taxonomic classification.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02353.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}],"value":"DSM 21410","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RCX02353.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000253517"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QPJS01000004","properties":[{"key":"ProteinId","value":"RCX02353.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_114366412.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BHZF01000005.1"}]},{"database":"AlphaFoldDB","id":"A0A368ZZJ2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00034","properties":[{"key":"RectionId","value":"UER00025"}]},{"database":"Proteomes","id":"UP000253517","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:0008837","properties":[{"key":"GoTerm","value":"F:diaminopimelate epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009085","properties":[{"key":"GoTerm","value":"P:L-lysine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.10.310.10","properties":[{"key":"EntryName","value":"Diaminopimelate Epimerase, Chain A, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00197","properties":[{"key":"EntryName","value":"DAP_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001653","properties":[{"key":"EntryName","value":"DAP_epimerase_DapF"}]},{"database":"NCBIfam","id":"TIGR00652","properties":[{"key":"EntryName","value":"DapF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31689:SF0","properties":[{"key":"EntryName","value":"DIAMINOPIMELATE EPIMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31689","properties":[{"key":"EntryName","value":"DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01678","properties":[{"key":"EntryName","value":"DAP_epimerase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54506","properties":[{"key":"EntryName","value":"Diaminopimelate epimerase-like"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MHIRFFKYQGTGNDFIIIDNRELTFPKTTELIQNMCHRKFGIGADGLILLENDEEVHFKMVYYNSDGRESTMCGNGGRCVAAFAKFIGIVDKRAVFRAVDGIHSAWIIDDVVSLELLDTSLPVKKEPGYYIDTGSPHLVIFKNDLDTIDVNLEGRKWRFDNTFENQGGVNVNFCSEPRGNTIYVRTYERGVESETLSCGTGVTAAALVTSYLYGINDSISVNTPGGDLSISFKRNSDKFEKISLTGQAKFVFEGKYWLS","length":259,"molWeight":29039,"crc64":"396F5FB8A0B66898","md5":"FB9264220DC0953C1D8DFC0E119250E4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":2,"Binding site":6,"Site":2},"uniParcId":"UPI000DF3BFD1"}}]}