{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DY18","uniProtkbId":"A0A420DY18_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02710.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF02710.1"}],"value":"C8N26_2699"}]}],"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":"RKF02710.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":512,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02710.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02710.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000014","properties":[{"key":"ProteinId","value":"RKF02710.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187673.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000014.1"}]},{"database":"AlphaFoldDB","id":"A0A420DY18","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000285780","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":"MNNTKYVFVTGGVTSSLGKGIIAASLAKLLQERGYSVTIQKLDPYINIDPGTLNPYEHGECYVTDDGAETDLDLGHYERYLNIPTSQANNVTTGRIYQSVINKERKGEFLGKTVQVIPHITDEIKNRVQILGNTGDFDIVITEIGGTVGDIESLPYIEAVRQLQWDLGEDNAVVVHLTLVPYLAAAGELKTKPTQHSVKMLMQSGVSPDILVCRSEHEISDDIKRKLALFCNVKKQNVIQSLDAETIYDVPNLMFKEGLDYVVLDKLRLSTRKQPKLTAWNRFLERHKNPTSTIEIGLVGKYVELHDSYKSITEAFIHAGAANKTKVNVRWIHSEELTPESAIQQLEGVDGVLVAPGFGDRGIEGKIAAVQYVRENNIPFLGICLGMQMAVIEFARNVLNLKDANSTEMNPKVAHPVINLMEEQKDVTDKGGTMRLGAWDCQLTQDSKVFEAYKQELISERHRHRYEYNNEYKEQLETAGMKTAGINPKTGLVEIVEIPTHPWFVGVQYHPEYKSTVLNPHPLFVSFIKAALKQSKK","length":537,"molWeight":60149,"crc64":"0F286528944759AA","md5":"519152A3296EC0E38914C570733A7E1B"},"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":"UPI000E75CD33"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYN9","uniProtkbId":"A0A420DYN9_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02928.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02928.1"}],"value":"C8N26_2575"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02928.1"}],"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":135,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Domain","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":732,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-101)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02928.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02928.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000012","properties":[{"key":"ProteinId","value":"RKF02928.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187577.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000012.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYN9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.520.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF6","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MKEAHTHSTSSNGKCPFSQGANTEIHDNIMEWWPKSLNLDILHQHDTKTNPLGNDFNYAEEFKKLDLEAVKNDLKTFMNDSQDWWPADWGTYGGLMIRMAWHAAGTYRVADGRGGSNTGNQRFAPLNSWPDNGNLDKARRLLWPIKKKYGNKLSWADLIILAGNMAYESMGFKTFGFAGGREDIWHPEKDIYWGSEKEWLAPTGSKGTRYSGDRDLENPLAAVMMGLIYVNPEGVDGKPDPLKTAHDVRETFKRMAMNDEETVALTAGGHTVGKAHGNGDAGALGQSPEGAEIEDQGFGWMNPKGNGNAADTVTSGLEGAWTTTPDKWNHTYFHLLLNHEWELKKSPAGAWQWEPVNMDEADKPTDAHNPNVKRNPIMTDADMAMKMDPEYRKISEKFYNDPASFEDAFARAWFKLTHRDLGPNTRYLGADAPAETLIWQDPVPTVDYTLNDSEIEELKEKLLNSGLSRTELINTAWDSARTYRGSDFRGGANGARIRLAPQKDWEGNEPTRLKKVLDKLTEIQSALSNKVSIADLIVLGGSAAVEKAAQEGGVNIKVPFTPGRGDATAEMTDAESFDVLEPLHDGYRNWQKKDYVVKPEELLLDRTQLMGLTAPEMTVLVGGMRVLGTNHGGTKHGVFTDNEGILSNDFFVNLTDMKYSWKPAGENLYNIVDRKTGSTKWTATRADLIFGSNSILRSYAEVYAQDDNKEKFVKDFVAAWTKVMNADRYDLA","length":732,"molWeight":81722,"crc64":"73CE3A3BEEA741F3","md5":"3DE0704235FD2A88D10CF87283740835"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI000E748472"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DZA0","uniProtkbId":"A0A420DZA0_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF03145.1"}],"value":"C8N26_2135"}]}],"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":"RKF03145.1"}],"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":14,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"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":32,"modifier":"EXACT"},"end":{"value":36,"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":83,"modifier":"EXACT"},"end":{"value":84,"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":113,"modifier":"EXACT"},"end":{"value":116,"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":114,"modifier":"EXACT"},"end":{"value":114,"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":137,"modifier":"EXACT"},"end":{"value":139,"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":166,"modifier":"EXACT"},"end":{"value":166,"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":174,"modifier":"EXACT"},"end":{"value":174,"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":181,"modifier":"EXACT"},"end":{"value":183,"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":197,"modifier":"EXACT"},"end":{"value":199,"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":225,"modifier":"EXACT"},"end":{"value":227,"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":234,"modifier":"EXACT"},"end":{"value":234,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":265,"modifier":"EXACT"},"end":{"value":268,"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":"UP000285780"}],"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-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000010","properties":[{"key":"ProteinId","value":"RKF03145.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A420DZA0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000285780","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":"MSKFDIRFMRKIKKIAVMTSGGDAPGMNAAIRSVVRTCAYYRTDCMGIYRGYQGLIEGDLIPLTARSVNNIIHKGGTILKSARSKDFRTKEGRQKAYESLKKNNVDALVVIGGDGSFTGGVIFNKEFNFPIIGIPGTIDNDISGTSHTLGYDTALNTAVEAIDKIRDTASSHNRLFFVEVMGRDAGFIALNAGVGAGAEEILIPEEDLGLERMLESLKKSRRSGKSSSIVVVSEGDKTGKNVFELADYVEENLPEYEVRVSVLGHMQRGGSPSCFDRVLASRLGVSAVELLLDGKTNLMVGLKDNKVISTDLEKAIKGQHNIDTELLRVSDIMTT","length":335,"molWeight":36433,"crc64":"37CAF8F3A8053195","md5":"D64712A56DD0EFF5B977CE0247BD3EAD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":14},"uniParcId":"UPI0004BA377E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DZG7","uniProtkbId":"A0A420DZG7_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03231.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF03231.1"}],"value":"C8N26_2221"}]}],"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":"RKF03231.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":399,"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":193,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"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":293,"modifier":"EXACT"},"end":{"value":293,"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":327,"modifier":"EXACT"},"end":{"value":327,"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":341,"modifier":"EXACT"},"end":{"value":341,"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":345,"modifier":"EXACT"},"end":{"value":345,"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":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03231.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03231.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000010","properties":[{"key":"ProteinId","value":"RKF03231.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187320.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000010.1"}]},{"database":"AlphaFoldDB","id":"A0A420DZG7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000285780","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":"MSVLSGKKVLLGVTAGIAAYKTANLVRLFIKSGAEVKVIMTPASKDFITPLTLSTLSKNPVHSTFYDKEDENELWNNHVDLGLWADLMLIAPATANTLSKMTNGTCDNLLLATYLSAKCPVYFAPAMDLDMYQHPSTKTSLESLQSFGNILIPATSGELASGLVGEGRMAEPEDIVDFIENDIVSKLPLRGKKILITAGPTYEAIDPVRFIGNHSSGKMGFEIAKTAANLGAEVILIAGPSHQQVNHSFIHRVDVKSAQDMYDACHQYYADVDVAVLSAAVADYRPKNVATQKIKKKEAALSIELEPTKDILKSLGEIKKKQLLVGFALETNDEVQNAKSKLTRKNLDFIVLNSLRDAGAGFATDTNKITIIDADLNEKSFDLKSKKEVSKDIVNEIIQKLDA","length":403,"molWeight":43871,"crc64":"132595FFBAB90347","md5":"DA63C0418FE0D8289E007F7D8CB5079C"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":5},"uniParcId":"UPI000E7580B2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420E040","uniProtkbId":"A0A420E040_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03297.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF03297.1"}],"value":"C8N26_2289"}]}],"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":"RKF03297.1"}],"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":16,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Transmembrane","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Coiled coil","location":{"start":{"value":585,"modifier":"EXACT"},"end":{"value":612,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Active site","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":238,"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":454,"modifier":"EXACT"},"end":{"value":454,"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":458,"modifier":"EXACT"},"end":{"value":458,"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":529,"modifier":"EXACT"},"end":{"value":529,"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":"RKF03297.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03297.1"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"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-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03297.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03297.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000010","properties":[{"key":"ProteinId","value":"RKF03297.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187368.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000010.1"}]},{"database":"AlphaFoldDB","id":"A0A420E040","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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":"MSDNKKNTPKFTFSSFWLYIPILIILLGLSFFNSGNLGSRNISKNEFTKILEANDIQKIVVENNNVAQIYLKPEAEKKEEHKKLAESPFFRKGSPLYSYNFGDLQNFENEIEKEKKENNLDFDKVNIERTSMMDTLISFLPFILLIAIWLFFMRRMSGAAGGGGAGGQIFNIGKSKAKLFDENTKVKTTFKNVAGLEGAKEEVQEIVDFLKSPEKYTKLGGKIPKGALLVGPPGTGKTLLAKAVAGEAGVPFFSLSGSDFVEMFVGVGASRVRDLFKQAQQKSPSIIFIDEIDAIGRARGKNSMTGGNDERENTLNQLLTEMDGFGTDTNVIVLAATNRADVLDKALMRAGRFDRQIYVDLPDLHERREIFNVHIKPLKLAENVNLEFLAQQTPGFSGADIANLCNEAALIAARKGKNAIEHQDFLDAVDRIVGGLEKKNKVITPKEKKVIAFHEAGHATVSWMLEHAAPLVKVTIVPRGQSLGAAWYLPEERKIVQTEQMLDEMCATMGGRAAEKLMFNKISTGALSDLEKVTKQARAMVTVYGLNDKVGNITYYDSSGNDAFVKPYSDATAQKIDEEISEIIENQYKRAIDILDENRDKLTELAELLLEKEVIFKDDLVKIFGDRPFGKEEEKTETTTEE","length":642,"molWeight":71472,"crc64":"856BCF4B8813120D","md5":"B1FF5E83407E087DC6C646A0743F9F85"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Transmembrane":2,"Domain":1,"Coiled coil":1,"Active site":1,"Binding site":4},"uniParcId":"UPI000E74AE19"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420E086","uniProtkbId":"A0A420E086_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2019-05-08","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03490.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF03490.1"}],"value":"C8N26_1878"}]}],"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":"RKF03490.1"}],"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":13,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":65,"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":62,"modifier":"EXACT"},"end":{"value":62,"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":125,"modifier":"EXACT"},"end":{"value":125,"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":129,"modifier":"EXACT"},"end":{"value":135,"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":158,"modifier":"EXACT"},"end":{"value":158,"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":161,"modifier":"EXACT"},"end":{"value":161,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":322,"modifier":"EXACT"},"end":{"value":322,"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":373,"modifier":"EXACT"},"end":{"value":373,"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":408,"modifier":"EXACT"},"end":{"value":412,"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":437,"modifier":"EXACT"},"end":{"value":437,"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":438,"modifier":"EXACT"},"end":{"value":438,"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":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03490.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03490.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000009","properties":[{"key":"ProteinId","value":"RKF03490.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187035.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000009.1"}]},{"database":"AlphaFoldDB","id":"A0A420E086","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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":"MKILEKILNVSQTREADKHTILKEDISSFALMGQASLAFVKAIEPLLQRSQKIAIIGGSGNNGGDGFAIARILRNKKYNIQPFLVQFKDILTPDCIINYEKLHDTIVINSTSEIPDFSEYDVIIDGIFGFGLSRPITGFTKQVIENINKAKKTVYAVDVPSGLYCDKLPDSETIVQADIVVSFQRPKLSFFFPENGNYVKNWKTVDIGLDEEFVQQQDSKHFILNEKIVDILTNRPRQSHKGDYGHTLLIAGSYGKMGAATLSSKACLRSGTGLLTTYVPKCGYQIVQSSIPEAMCITDENEEFVTQLPEISKYDVIGIGPGLDTNEKTIRVVKKLLSESKNPLVIDADAINIIAQNEELKSLLPKNSILTPHVKEFDRLVGNSDTSTERFQKQLEFSAKYQCVVVLKNAYTVISSPEGNLYFNTSGNQGMATGGSGDVLTGIITGLLAQNYTPLHAALLGVFFHGKAGDEAACKKGYKALIASDIIDALRIEKN","length":495,"molWeight":54444,"crc64":"333C964E6DCCB150","md5":"33854FC2B5D954CA83306143BA48D0C9"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI000E743D41"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420E1H0","uniProtkbId":"A0A420E1H0_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03918.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF03918.1"}],"value":"C8N26_1549"}]}],"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":"RKF03918.1"}],"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":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00388"}]},{"type":"Active site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00406"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"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":261,"modifier":"EXACT"},"end":{"value":261,"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":265,"modifier":"EXACT"},"end":{"value":265,"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":"UP000285780"}],"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-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03918.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF03918.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000008","properties":[{"key":"ProteinId","value":"RKF03918.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120186770.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000008.1"}]},{"database":"AlphaFoldDB","id":"A0A420E1H0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00359","properties":[{"key":"RectionId","value":"UER00478"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019171","properties":[{"key":"GoTerm","value":"F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0103117","properties":[{"key":"GoTerm","value":"F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01288","properties":[{"key":"EntryName","value":"FabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000001","properties":[{"key":"EntryName","value":"3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.20","properties":[{"key":"EntryName","value":"lpxc deacetylase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1700.10","properties":[{"key":"EntryName","value":"lpxc deacetylase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00406","properties":[{"key":"EntryName","value":"FabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00388","properties":[{"key":"EntryName","value":"LpxC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013114","properties":[{"key":"EntryName","value":"FabA_FabZ"}]},{"database":"InterPro","id":"IPR010084","properties":[{"key":"EntryName","value":"FabZ"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR004463","properties":[{"key":"EntryName","value":"UDP-acyl_GlcNac_deAcase"}]},{"database":"InterPro","id":"IPR011334","properties":[{"key":"EntryName","value":"UDP-acyl_GlcNac_deAcase_C"}]},{"database":"InterPro","id":"IPR015870","properties":[{"key":"EntryName","value":"UDP-acyl_N-AcGlcN_deAcase_N"}]},{"database":"NCBIfam","id":"NF000582","properties":[{"key":"EntryName","value":"fabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01750","properties":[{"key":"EntryName","value":"fabZ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00325","properties":[{"key":"EntryName","value":"lpxC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009667","properties":[{"key":"EntryName","value":"PRK13188.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33694","properties":[{"key":"EntryName","value":"UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33694:SF1","properties":[{"key":"EntryName","value":"UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07977","properties":[{"key":"EntryName","value":"FabA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03331","properties":[{"key":"EntryName","value":"LpxC"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKKQKTIQNEITLSGVGLHTGNEVTMVFKPAPENHGFAFKRVDLEGEPVIEAKAEYVTNTQRGTNLEKNGVQIQTSEHVLAAAVGLDIDNLLIEVNASEPPIMDGSSKFFIEALEEAGIIEQEAEVEEYVVKEIISYKDEVTGSEIILMPADEYQITTMVDFGTKILGTQNATLDKISDFKEEISAARTFSFLHEIEMLLENDLIKGGDLNNAIVYVDKELSDSTMQKLKKAFNKENITVKPNGVLDNLTLHWANEAARHKLLDVIGDLALTGTRVRGKVIANKPGHSVNTTFAKKLAKIIKQEKRNNVPTYDLNQPPLMDIHKIMDILPHRPPFLLIDRIIELSDKHVVGMKNVTMNEDFFVGHFPGAPVMPGVLQVEAMAQCGGVLVLNTVPDPENYLTYFMKMDNVKFKQKVLPGDTLIFKSELITPIRRGIAHMQAYAYANGKLVCEAELMAQISKVK","length":463,"molWeight":51499,"crc64":"DED09425414D7A41","md5":"38A33A6AAD0967C117AAC88C1951A592"},"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":"UPI000E7347E1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420E1T3","uniProtkbId":"A0A420E1T3_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04085.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF04085.1"}],"value":"C8N26_0744"}]}],"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":"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":"RKF04085.1"}],"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":"HAMAP-Rule","id":"MF_00985"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04085.1"}],"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":"UP000285780"}],"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-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04085.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04085.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000007","properties":[{"key":"ProteinId","value":"RKF04085.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120186112.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A420E1T3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00046","properties":[{"key":"RectionId","value":"UER00506"}]},{"database":"Proteomes","id":"UP000285780","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:SF103","properties":[{"key":"EntryName","value":"AMINOTRANSFERASE CLASS I_CLASSII DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693","properties":[{"key":"EntryName","value":"CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00155","properties":[{"key":"EntryName","value":"Aminotran_1_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYGKIKEQLQQEIQDIKDAGLYKSERIITSSQDAVIKISTGEEVINFCANNYLGLSNNPEVIQAAKDTMDTHGFGMSSVRFICGTQDIHKQLEQKIADFYTTEDTILYAAAFDANGGVFEPLLTSEDAIISDSLNHASIIDGVRLCKAARYRYNNNDMASLEEQLIEANKHNHRFKIIVTDGVFSMDGIVAKLDDICDLADKYDAMVMVDECHAAGFIGKTGRGTVELKNVMDRVDIVTGTLGKALGGAMGGYTTGKKEIIEILRQRSRPYLFSNSLAPAIVGASLKVFDLLSNDTTLRDKLEWNTNYFRSEMEKAGFDLVGADAAIVPVMLYDAKLSQVMANKLLEEGIYVIGFFYPVVPKEQARIRVQLSAAHEKEHLDKAIKAFIKVGKELKVI","length":397,"molWeight":43961,"crc64":"CEE76DB249EA27E7","md5":"E5664635DF09E6E2F5BF6F4214650254"},"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":"UPI000E71104C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420E2V4","uniProtkbId":"A0A420E2V4_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04380.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF04380.1"}],"value":"C8N26_1047"}]}],"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":"RKF04380.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"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-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04380.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04380.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000007","properties":[{"key":"ProteinId","value":"RKF04380.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_028892447.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000007.1"}]},{"database":"AlphaFoldDB","id":"A0A420E2V4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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":"MTAKKKDIRALTKEQLRDFFVENGDKAFRGNQVYEWLWHKAAHSFNDMTSLSKATRQMLDDNFVINHIEVDTMQRSNDGTIKNAIKLHDGLIVESVLIPTETRTTACVSSQVGCSLDCKFCATARLKRMRNLNADEIYDQVVAIDKQSRLYHNHKLSNIVFMGMGEPLMNYNNVIKAIDKITSPEGLGMAARRITVSTSGVPKIIKKMADDEVRFNLAVSLHSAIEEVRTSIMPFNATFPLKDLREALEYWYEKTKRKVTYEYVVWNGINDRKEDINALVEFCKYIPCKVNLIEYNPIDDGEFQQASERAINNYISNLEMNDIVVNVRRSRGKDIDAACGQLANKS","length":346,"molWeight":39520,"crc64":"6AB95F640FABE0B5","md5":"A2655B776714FAD85D45D8A6A55C5D1F"},"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":"UPI00048E2279"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420E3Y5","uniProtkbId":"A0A420E3Y5_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04750.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"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":"RKF04750.1"}],"value":"C8N26_0139"}]}],"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":"RKF04750.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04750.1"}],"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":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04750.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF04750.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000006","properties":[{"key":"ProteinId","value":"RKF04750.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120185602.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000006.1"}]},{"database":"AlphaFoldDB","id":"A0A420E3Y5","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKNLKNILYKVAVKEVYGNTDIDINNIQFDSRQVQDNDVFVAQKGVTVDGHQYIEKAVSLGAKAVICEEVPEKRSEQITYIKVEDSNVALAIIAANYYNNPSKSLQLVGVTGTNGKTTIASLLYQLFKKAGYKVGLLSTVKIMVDEIEYKATHTTPNSVAINEYLSKMVDEGVEYCFMEVSSHGIHQKRTEGLEFVGGVFTNLSHDHLDYHETFAEYRDVKKSFFDSLPKSAFALVNIDDKNGQIMLQNTKAIKQTYALKTIGDFKAKVLEKRFSGTLLTINGVEVWTKLIGEFNAYNLLAIYGVAELLGLEKLEILRIVSELESVSGRFQYTISNEGVTAIVDYAHTPDALKNVLQTINDIRTGNETVITVVGCGGDRDATKRPKMALIASQLSNQAIFTSDNPRTEDPQSIIDQMEEGVAAENYKKTLSILDRRQAIKTACKLAKTGDIILIAGKGHETYQEINGIRHHFDDLEEITNCFNQLKKH","length":488,"molWeight":54385,"crc64":"419DB0B8FFB38467","md5":"8FFD06E1096709DA92CCE7ABD92C4D73"},"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":"UPI000E73A3C0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DXZ5","uniProtkbId":"A0A420DXZ5_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":19,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02706.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Fumarate hydratase class II"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Fumarase C"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"4.2.1.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Aerobic fumarase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Iron-independent fumarase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"fumC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02706.1"}],"value":"C8N26_2695"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-malate = fumarate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12460"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15589"},{"database":"ChEBI","id":"CHEBI:29806"}],"ecNumber":"4.2.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009084"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Belongs to the class-II fumarase/aspartase family. Fumarase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02706.1"}],"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":12,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Fumarate lyase-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00206"}]},{"type":"Domain","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Fumarase C C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10415"}]},{"type":"Active site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]},{"type":"Active site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02706.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02706.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000014","properties":[{"key":"ProteinId","value":"RKF02706.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_028891108.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000014.1"}]},{"database":"AlphaFoldDB","id":"A0A420DXZ5","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00223","properties":[{"key":"RectionId","value":"UER01007"}]},{"database":"Proteomes","id":"UP000285780","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:0004333","properties":[{"key":"GoTerm","value":"F:fumarate hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006106","properties":[{"key":"GoTerm","value":"P:fumarate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006108","properties":[{"key":"GoTerm","value":"P:malate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006099","properties":[{"key":"GoTerm","value":"P:tricarboxylic acid cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01362","properties":[{"key":"EntryName","value":"Fumarase_classII"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.40.30:FF:000002","properties":[{"key":"EntryName","value":"Fumarate hydratase class II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.275.10:FF:000001","properties":[{"key":"EntryName","value":"Fumarate hydratase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.200.10:FF:000001","properties":[{"key":"EntryName","value":"Fumarate hydratase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.40.30","properties":[{"key":"EntryName","value":"Fumarase/aspartase (C-terminal domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.200.10","properties":[{"key":"EntryName","value":"Fumarase/aspartase (Central domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.275.10","properties":[{"key":"EntryName","value":"Fumarase/aspartase (N-terminal domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00743","properties":[{"key":"EntryName","value":"FumaraseC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005677","properties":[{"key":"EntryName","value":"Fum_hydII"}]},{"database":"InterPro","id":"IPR024083","properties":[{"key":"EntryName","value":"Fumarase/histidase_N"}]},{"database":"InterPro","id":"IPR018951","properties":[{"key":"EntryName","value":"Fumarase_C_C"}]},{"database":"InterPro","id":"IPR022761","properties":[{"key":"EntryName","value":"Fumarate-Lyase-like_N"}]},{"database":"InterPro","id":"IPR020557","properties":[{"key":"EntryName","value":"Fumarate_lyase_CS"}]},{"database":"InterPro","id":"IPR000362","properties":[{"key":"EntryName","value":"Fumarate_lyase_fam"}]},{"database":"InterPro","id":"IPR008948","properties":[{"key":"EntryName","value":"L-Aspartase-like"}]},{"database":"NCBIfam","id":"TIGR00979","properties":[{"key":"EntryName","value":"fumC_II"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008909","properties":[{"key":"EntryName","value":"PRK12273.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11444","properties":[{"key":"EntryName","value":"ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11444:SF1","properties":[{"key":"EntryName","value":"FUMARATE HYDRATASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10415","properties":[{"key":"EntryName","value":"FumaraseC_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00206","properties":[{"key":"EntryName","value":"Lyase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00145","properties":[{"key":"EntryName","value":"ARGSUCLYASE"}]},{"database":"PRINTS","id":"PR00149","properties":[{"key":"EntryName","value":"FUMRATELYASE"}]},{"database":"SUPFAM","id":"SSF48557","properties":[{"key":"EntryName","value":"L-aspartase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00163","properties":[{"key":"EntryName","value":"FUMARATE_LYASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKYRIEKDTMGQVEVPADKYWGAQTERSRNNFKIGPAASMPLEVVYGFAYLKKAAAYTNAELGVLATEKRDLIAQVCDEILEGKHDNQFPLVIWQTGSGTQSNMNVNEVIANRAHEIAGKVIGEGEKTIQPNDDVNKSQSSNDTFPTGMHIAAYKKIVEVTIPGVEQLRDTLQAKAEAFKDVVKIGRTHLMDATPLTLGQEFSGYVAQLNFGLNALKNTLAHLAQLALGGTAVGTGLNTPAGYDVLVAKYIAEFTGLPFVTAENKFEALAAHDALVETHGALKQLAVSLNKIANDIRLMASGPRSGIGEIIIPANEPGSSIMPGKVNPTQAEAMTMVCAQVMGNDVAVTVGGTQGHYELNVFKPMMAANVLQSAQLIGDACVSFDVNCAAGIEPNQTRITELLNNSLMLVTALNTKIGYYKAAEIANTAHANGTTLKEEAVRLGYVTPEQYDEWVKPEDMIGSLK","length":466,"molWeight":50086,"crc64":"E0E6DD9E39F78EF9","md5":"6EF1E33DCD9B70DF9D5E45711F83591D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":5,"Site":1},"uniParcId":"UPI0004901013"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DY29","uniProtkbId":"A0A420DY29_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":18,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02720.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Phosphopantetheine adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"2.7.7.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Dephospho-CoA pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Pantetheine-phosphate adenylyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"PPAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"coaD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02720.1"}],"value":"C8N26_2709"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19801"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57328"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"2.7.7.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029346"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Belongs to the bacterial CoaD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02720.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022993"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"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_00151"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"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_00151"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02720.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02720.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000014","properties":[{"key":"ProteinId","value":"RKF02720.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_028891124.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000014.1"}]},{"database":"AlphaFoldDB","id":"A0A420DY29","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00355"}]},{"database":"Proteomes","id":"UP000285780","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:0004595","properties":[{"key":"GoTerm","value":"F:pantetheine-phosphate adenylyltransferase 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":"cd02163","properties":[{"key":"EntryName","value":"PPAT"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00151","properties":[{"key":"EntryName","value":"PPAT_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004821","properties":[{"key":"EntryName","value":"Cyt_trans-like"}]},{"database":"InterPro","id":"IPR001980","properties":[{"key":"EntryName","value":"PPAT"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR01510","properties":[{"key":"EntryName","value":"coaD_prev_kdtB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00125","properties":[{"key":"EntryName","value":"cyt_tran_rel"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21342","properties":[{"key":"EntryName","value":"PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21342:SF1","properties":[{"key":"EntryName","value":"PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01467","properties":[{"key":"EntryName","value":"CTP_transf_like"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01020","properties":[{"key":"EntryName","value":"LPSBIOSNTHSS"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRAIFPGSFDPITLGHVDIIERGVTLFDELIIAIGINADKKYMFSLEERKRFIEETFKHEPKIKVLTYSGLTVNFCKEQDAQFILRGLRNPADFEFEKAIAHTNRKLSEIETVFLLTSSGKSYISSSIVRDVIRNEGDYTGLVPDAVRI","length":150,"molWeight":17102,"crc64":"8047594A4BB55EFE","md5":"CF6908BF83AC9D2116AD44BC241E43F3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":9,"Site":1},"uniParcId":"UPI00048E5EA7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DY36","uniProtkbId":"A0A420DY36_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02721.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012216"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"D-alanine--D-alanine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012216"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"6.3.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"D-Ala-D-Ala ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"D-alanylalanine synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"ddl"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02721.1"}],"value":"C8N26_2710"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"Cell wall formation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 D-alanine + ATP = D-alanyl-D-alanine + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11224"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57822"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047614"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"value":"Binds 2 magnesium or manganese ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010871"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"value":"Belongs to the D-alanine--D-alanine ligase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02721.1"}],"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":121,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Active site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-1"}]},{"type":"Active site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-1"}]},{"type":"Active site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-1"}]},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"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_00047"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR039102-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00047"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02721.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02721.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000014","properties":[{"key":"ProteinId","value":"RKF02721.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187681.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000014.1"}]},{"database":"AlphaFoldDB","id":"A0A420DY36","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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:0008716","properties":[{"key":"GoTerm","value":"F:D-alanine-D-alanine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"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":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00047","properties":[{"key":"EntryName","value":"Dala_Dala_lig"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR000291","properties":[{"key":"EntryName","value":"D-Ala_lig_Van_CS"}]},{"database":"InterPro","id":"IPR005905","properties":[{"key":"EntryName","value":"D_ala_D_ala"}]},{"database":"InterPro","id":"IPR011095","properties":[{"key":"EntryName","value":"Dala_Dala_lig_C"}]},{"database":"InterPro","id":"IPR011127","properties":[{"key":"EntryName","value":"Dala_Dala_lig_N"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01205","properties":[{"key":"EntryName","value":"D_ala_D_alaTIGR"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002378","properties":[{"key":"EntryName","value":"PRK01372.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002527","properties":[{"key":"EntryName","value":"PRK01966.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23132","properties":[{"key":"EntryName","value":"D-ALANINE--D-ALANINE LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23132:SF23","properties":[{"key":"EntryName","value":"D-ALANINE--D-ALANINE LIGASE B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07478","properties":[{"key":"EntryName","value":"Dala_Dala_lig_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01820","properties":[{"key":"EntryName","value":"Dala_Dala_lig_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF039102","properties":[{"key":"EntryName","value":"Ddl/VanB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00844","properties":[{"key":"EntryName","value":"DALA_DALA_LIGASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKNIAIIMGGYSSEVGISLKSGNVVYKHLNKEKYNPYRVHILKDKWVLVDDDENEHPINKHDFSAEVNGTNISFDAVFNAIHGTPGENGVILAYFNLIGLKHTSAPFYQMALTFNKRDTLSVVKEYGIPAATSVYLNKGDKINTNTIIEKVGLPCFVKPNGAGSSFGISKVYTQEELIPAIEKAYEEDSEILIESFLDGTEVSVGVIQYKGETKVLPITEIVSDNDFFDYKAKYEGESQEITPARLTEAQEKSVNDIAKRVYEILNMSGFSRSEYILVNDIPHFLEMNTVPGLTEASILPQQANHAGISLTELFGNAIEMALKN","length":325,"molWeight":36070,"crc64":"9A4DEBD926E9E732","md5":"D809298D252AC937FD6927C8CC648DE5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":3,"Binding site":3},"uniParcId":"UPI000E74E1D2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DY75","uniProtkbId":"A0A420DY75_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02743.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"tRNA modification GTPase MnmE"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"3.6.-.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"mnmE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"trmE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02743.1"}],"value":"C8N26_2732"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Homodimer. Heterotetramer of two MnmE and two MnmG subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011043"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003313"}],"value":"Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02743.1"}],"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":222,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"TrmE-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51709"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"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_00379"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"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_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02743.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02743.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000014","properties":[{"key":"ProteinId","value":"RKF02743.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187698.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000014.1"}]},{"database":"AlphaFoldDB","id":"A0A420DY75","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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: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:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030955","properties":[{"key":"GoTerm","value":"F:potassium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0002098","properties":[{"key":"GoTerm","value":"P:tRNA wobble uridine modification"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04164","properties":[{"key":"EntryName","value":"trmE"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd14858","properties":[{"key":"EntryName","value":"TrmE_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1360.120:FF:000003","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001376","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE"},{"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":"3.30.1360.120","properties":[{"key":"EntryName","value":"Probable tRNA modification gtpase trme, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.430","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00379","properties":[{"key":"EntryName","value":"GTPase_MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR031168","properties":[{"key":"EntryName","value":"G_TrmE"}]},{"database":"InterPro","id":"IPR006073","properties":[{"key":"EntryName","value":"GTP-bd"}]},{"database":"InterPro","id":"IPR018948","properties":[{"key":"EntryName","value":"GTP-bd_TrmE_N"}]},{"database":"InterPro","id":"IPR004520","properties":[{"key":"EntryName","value":"GTPase_MnmE"}]},{"database":"InterPro","id":"IPR027368","properties":[{"key":"EntryName","value":"MnmE_dom2"}]},{"database":"InterPro","id":"IPR025867","properties":[{"key":"EntryName","value":"MnmE_helical"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005225","properties":[{"key":"EntryName","value":"Small_GTP-bd"}]},{"database":"InterPro","id":"IPR027266","properties":[{"key":"EntryName","value":"TrmE/GcvT-like"}]},{"database":"NCBIfam","id":"NF003661","properties":[{"key":"EntryName","value":"mnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00450","properties":[{"key":"EntryName","value":"mnmE_trmE_thdF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00231","properties":[{"key":"EntryName","value":"small_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42714","properties":[{"key":"EntryName","value":"TRNA MODIFICATION GTPASE GTPBP3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42714:SF2","properties":[{"key":"EntryName","value":"TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01926","properties":[{"key":"EntryName","value":"MMR_HSR1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12631","properties":[{"key":"EntryName","value":"MnmE_helical"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10396","properties":[{"key":"EntryName","value":"TrmE_N"},{"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":"PS51709","properties":[{"key":"EntryName","value":"G_TRME"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIQNDTIIALATPAGVGAIAVIRLSGEKSIKIVDSFFSSIKKNKSLLNQKSHTLHLGHIVNNGVVIDQVLVSIFKNPHSYTGEDVVEISCHGSSFIQQEIIQLFLQNGCRMADNGEFTMRAFLNGKMDLSQAEAVADVIASNSAASHQMAIQQMRGGITNELKELRAQLLDFAALIELELDFSGEDVEFADRTKFKELVAKISAVLKRLIDSFAFGNAMKNGIPVAIIGEPNVGKSTLLNALLNEEKAIVSDIAGTTRDAIEDELIIDGVVFRFIDTAGIRETEDVVENIGIKKAYEKAENAQLIIFLIDSNKYIHSKELFLEEIDTIHQRFPNKRLLVIANKIDTLSCHDSSILQSDIENLILLSAKQNIGIDELKKELISLVNTGALSNNETIVTNSRHFEALNHALESINSVKNGIELDISSDLFAIDIRECLRHLGNITGEYDVDKDILGHIFGNFCIGK","length":464,"molWeight":51054,"crc64":"D19C087263701158","md5":"62088B40C1CDE63C175AE837BC58791B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":17},"uniParcId":"UPI000E750163"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DY80","uniProtkbId":"A0A420DY80_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02794.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"6.3.2.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"value":"D-alanyl-D-alanine-adding enzyme"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"value":"murF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02794.1"}],"value":"C8N26_2642"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28374"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57822"},{"database":"ChEBI","id":"CHEBI:61386"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"value":"Belongs to the MurCDEF family. MurF subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02794.1"}],"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":92,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"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_02019"}],"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_02019"}],"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_02019"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02794.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02794.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02794.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A420DY80","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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:0047480","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008766","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0071555","properties":[{"key":"GoTerm","value":"P:cell wall organization"},{"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":"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_02019","properties":[{"key":"EntryName","value":"MurF"},{"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":"IPR051046","properties":[{"key":"EntryName","value":"MurCDEF_CellWall_CoF430Synth"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005863","properties":[{"key":"EntryName","value":"UDP-N-AcMur_synth"}]},{"database":"NCBIfam","id":"TIGR01143","properties":[{"key":"EntryName","value":"murF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43024","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43024:SF1","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE"},{"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":"MRFFYFYKMKIEDLYQLYSIHGLVDTDTRNIRQNTIFFALKGENFNGNKFAEEAIDNGASYAVVDEEAYNTSEKTILVDNVLETLQKLANYHRNQLGLPIIALTGSNGKTTTKELINAVLSTKYKTTATVGNLNNHIGVPLTLLSMNRDTEIGIVEMGANHHKEIAFLSEIAGPDYGYITNFGSAHLEGFGSLEGVVKAKSELYEYLRKHNKKVIVNPNDAKQIEHTKGMDSVWFSNDIKYLDADPLVRFSYQEKIITSNLIGVYNFANISAAITIGNYFKVTPEQIKEAIENYIPSNNRSQVIKTERNTIILDAYNANPTSMKAALESFEALKSAHKTIIIGDMFELGEYSSKEHQKIADIVQEFNFNSVFLVGENFYKTTTEFKKFKNFTELAEYLKFNPINKSTILVKGSRGMALERVVEFC","length":425,"molWeight":48073,"crc64":"00BADD965C9498F7","md5":"A1874DC6DE14C84F2A3A3EC65C5830D0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Binding site":1},"uniParcId":"UPI000FF2E529"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DY81","uniProtkbId":"A0A420DY81_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097693"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Transcription termination factor Rho"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00767"}],"value":"3.6.4.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"ATP-dependent helicase Rho"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"rho"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02769.1"}],"value":"C8N26_2615"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Facilitates transcription termination from RNA polymerase (RNAP) by binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, translocation in a 5'-3' direction on the RNA (toward RNAP), and release of the RNA from the DNA template"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Plays a major role in reduction of R-loop formation across the genome; R-loops can be generated by annealing of untranslated, (often antisense) RNA to upstream DNA"}],"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":"ARBA","id":"ARBA00049360"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Homohexamer. The homohexamer assembles into a catalytically inactive open ring structure; the active homohexamer is a closed ring which encircles RNA. Contacts RNA polymerase (RNAP) via its C-terminal domains, allowing RNA to pass through the central channel"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"The N-terminus consists of a helical bundle and an OB-fold which form the primary RNA-binding site (PBS, part of Rho RNA-BD) on the surface of the hexameric ring. The N-terminus is joined by a linker to the C-terminal domain, which has a RecA-type fold. Six C-terminal domains form a central channel through which single-stranded (ss)RNA passes; ATP binds between the protomers. The secondary RNA-binding site (SBS) is formed by Q- and R-loops in the center of the ring which recognize pyrimidine-rich RNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01203"}],"value":"Belongs to the Rho family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02769.1"}],"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":170,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Rho RNA-BD","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51856"}]},{"type":"Region","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":398,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Q-loop","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}]},{"type":"Motif","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"R-loop","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}]},{"type":"Compositional bias","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":485,"modifier":"EXACT"},"end":{"value":485,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":486,"modifier":"EXACT"},"end":{"value":486,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022472"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0806","category":"Biological process","name":"Transcription termination"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02769.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187607.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DY81","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008186","properties":[{"key":"GoTerm","value":"F:ATP-dependent activity, acting on RNA"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004386","properties":[{"key":"GoTerm","value":"F:helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006353","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription termination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04459","properties":[{"key":"EntryName","value":"Rho_CSD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01128","properties":[{"key":"EntryName","value":"rho_factor_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.720.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01884","properties":[{"key":"EntryName","value":"Rho"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR011129","properties":[{"key":"EntryName","value":"CSD"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011112","properties":[{"key":"EntryName","value":"Rho-like_N"}]},{"database":"InterPro","id":"IPR041703","properties":[{"key":"EntryName","value":"Rho_factor_ATP-bd"}]},{"database":"InterPro","id":"IPR036269","properties":[{"key":"EntryName","value":"Rho_N_sf"}]},{"database":"InterPro","id":"IPR011113","properties":[{"key":"EntryName","value":"Rho_RNA-bd"}]},{"database":"InterPro","id":"IPR004665","properties":[{"key":"EntryName","value":"Term_rho"}]},{"database":"NCBIfam","id":"NF006886","properties":[{"key":"EntryName","value":"rho"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00767","properties":[{"key":"EntryName","value":"rho"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46425","properties":[{"key":"EntryName","value":"TRANSCRIPTION TERMINATION FACTOR RHO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46425:SF1","properties":[{"key":"EntryName","value":"TRANSCRIPTION TERMINATION FACTOR RHO"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07498","properties":[{"key":"EntryName","value":"Rho_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07497","properties":[{"key":"EntryName","value":"Rho_RNA_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00357","properties":[{"key":"EntryName","value":"CSP"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00959","properties":[{"key":"EntryName","value":"Rho_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF68912","properties":[{"key":"EntryName","value":"Rho N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51856","properties":[{"key":"EntryName","value":"RHO_RNA_BD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFEISELKTKKLADLQVIAKTIGLTKFSQLKKLDLVYKILDAQAEASANEAKPKAEKPKRKRIAKDDAPRDTSKQQQDNNPVKKVEAKEEVEKTETVVNNPVKKVEDKKQYPQSQSNEDKKQQQPQKQHTKNQNRGNKSNKNQNQNQNTSKQHHKSGNKYRDPDFEFDGIIESEGVLEMMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDTVRGNVRPPKEGEKYFPLIRVSKINGLNPNIVRDRVSFEHLTPLFADEKFNLAEKGSSLSTRIIDLFSPIGKGQRGMIVAQPKTGKTMLLKDVANAIAANHPEVYQIVLLIDERPEEVTDMQRSVRGEVVASTFDEPADKHVRVANIVLEKAKRLVECGHDVVILLDSITRLARAYNTVAPASGKILSGGIDANALHKPKRFFGAARNIENGGSLTIIATALTETGSKMDEVIFEEFKGTGNMELQLERNIANRRIYPAIDLIKSSTRRDDLLLDEKTVQRMWVLRKYLADMNPIEAMEFIQDRIKRSLNNDEFLISMNG","length":537,"molWeight":60622,"crc64":"E188D6DCE8108BCF","md5":"D85FA751E92D0F3B3AAF5FE4FC7C2442"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Motif":2,"Compositional bias":3,"Binding site":6},"uniParcId":"UPI000E74E42F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYA6","uniProtkbId":"A0A420DYA6_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02775.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridine synthase A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"5.4.99.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridine(38-40) synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridylate synthase I"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA-uridine isomerase I"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"truA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02775.1"}],"value":"C8N26_2621"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22376"},{"database":"Rhea","id":"RHEA-COMP:10085"},{"database":"Rhea","id":"RHEA-COMP:10087"},{"database":"ChEBI","id":"CHEBI:65314"},{"database":"ChEBI","id":"CHEBI:65315"}],"ecNumber":"5.4.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003792"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009375"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003792"}],"value":"Belongs to the tRNA pseudouridine synthase TruA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02775.1"}],"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":148,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Pseudouridine synthase I TruA alpha/beta","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01416"}]},{"type":"Active site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001430-1"}]},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001430-2"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02775.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02775.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02775.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187612.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYA6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0160147","properties":[{"key":"GoTerm","value":"F:tRNA pseudouridine(38-40) synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0031119","properties":[{"key":"GoTerm","value":"P:tRNA pseudouridine synthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02570","properties":[{"key":"EntryName","value":"PseudoU_synth_EcTruA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.580:FF:000001","properties":[{"key":"EntryName","value":"tRNA pseudouridine synthase A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.660","properties":[{"key":"EntryName","value":"Pseudouridine synthase I, catalytic domain, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.580","properties":[{"key":"EntryName","value":"Pseudouridine synthase I, catalytic domain, N-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00171","properties":[{"key":"EntryName","value":"TruA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020103","properties":[{"key":"EntryName","value":"PsdUridine_synth_cat_dom_sf"}]},{"database":"InterPro","id":"IPR001406","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA"}]},{"database":"InterPro","id":"IPR020097","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA_a/b_dom"}]},{"database":"InterPro","id":"IPR020095","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA_C"}]},{"database":"InterPro","id":"IPR020094","properties":[{"key":"EntryName","value":"TruA/RsuA/RluB/E/F_N"}]},{"database":"NCBIfam","id":"TIGR00071","properties":[{"key":"EntryName","value":"hisT_truA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11142","properties":[{"key":"EntryName","value":"PSEUDOURIDYLATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11142:SF0","properties":[{"key":"EntryName","value":"TRNA PSEUDOURIDINE SYNTHASE-LIKE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01416","properties":[{"key":"EntryName","value":"PseudoU_synth_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001430","properties":[{"key":"EntryName","value":"tRNA_psdUrid_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55120","properties":[{"key":"EntryName","value":"Pseudouridine synthase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRYFIQLAYNGKNYHGWQIQPHAISVQEVINKAISTILRQEINIVGAGRTDAGVHASQMFAHFDVTSPLNDDFTYKLNAILPDDVVIFNTLLVHKDAHARFDANSRNYEYKIWLGRNPFLLETSWQLHHQQLNIELMNKAAAILYEYEDFECFSKVKTDVNTFNCTVTNAEWIKKGNELTFHISANRFLRNMVRAIVGTLIDVGLEKITIDDFKKIIESKNRSKAGASAPAKGLFLTAVTYDYI","length":244,"molWeight":27906,"crc64":"206DA475D8F39E55","md5":"42F87D11BCDC8214600A863EFEDA0315"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":1},"uniParcId":"UPI000E75684F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYB1","uniProtkbId":"A0A420DYB1_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2019-05-08","entryVersion":19,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02790.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Phosphatidylserine decarboxylase proenzyme"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Phosphatidylserine decarboxylase alpha chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Phosphatidylserine decarboxylase beta chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"psd"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02790.1"}],"value":"C8N26_2638"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type II sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02790.1"}],"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":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"featureId":"PRO_5023490175"},{"type":"Chain","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"featureId":"PRO_5023490174"},{"type":"Active site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]},{"type":"Active site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]},{"type":"Active site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]},{"type":"Active site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]},{"type":"Site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]},{"type":"Modified residue","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"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_00663"}],"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_00663"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00663"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02790.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02790.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02790.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187623.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYB1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00558","properties":[{"key":"RectionId","value":"UER00616"}]},{"database":"Proteomes","id":"UP000285780","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:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_00663","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033179","properties":[{"key":"EntryName","value":"PSD_type2_pro"}]},{"database":"NCBIfam","id":"NF001941","properties":[{"key":"EntryName","value":"PRK00723.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF17","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIKFIDRKTGKIITETPPGEGYLKLLYNNPFGKMALLLLVKRKFLSSWYGKLMNKPNSINKINSFVRELQIDMNEAERPSEDYISFNDFFYRKLKPDARPIEEGFVSPGDGKMLAFKNISDIQNFFVKGRKFTLEEFLGNKELATKHKDDSLIILRLAPNDYHRYHFPYDGIPSEVTKIKGRYFSVSPYALASNFTKVFCENKREFCTLKTQNKGDIIIAPVGATMVGSIIETYTPNTKVKKGDEMGYFAFGGSTIVLLVDSSKITIDEDILANTKNKMETFVKMGEQIGK","length":292,"molWeight":33319,"crc64":"7E9F1F9EAE5111D5","md5":"F38FCC9B1BAC36CCE639FAB71467F53B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI000E76E189"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYB3","uniProtkbId":"A0A420DYB3_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02799.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"GMP synthase [glutamine-hydrolyzing]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"6.3.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"GMP synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Glutamine amidotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"guaA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02799.1"}],"value":"C8N26_2647"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002332"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Catalyzes the synthesis of GMP from XMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP + diphosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:58115"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005153"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02799.1"}],"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":195,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"GMPS ATP-PPase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51553"}]},{"type":"Active site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00886"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0332","category":"Biological process","name":"GMP biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02799.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02799.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02799.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187629.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYB3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00189","properties":[{"key":"RectionId","value":"UER00296"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003921","properties":[{"key":"GoTerm","value":"F:GMP synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01742","properties":[{"key":"EntryName","value":"GATase1_GMP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01997","properties":[{"key":"EntryName","value":"GMP_synthase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.10:FF:000002","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000047","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing] subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00344","properties":[{"key":"EntryName","value":"GMP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR001674","properties":[{"key":"EntryName","value":"GMP_synth_C"}]},{"database":"InterPro","id":"IPR004739","properties":[{"key":"EntryName","value":"GMP_synth_GATase"}]},{"database":"InterPro","id":"IPR022955","properties":[{"key":"EntryName","value":"GMP_synthase"}]},{"database":"InterPro","id":"IPR025777","properties":[{"key":"EntryName","value":"GMPS_ATP_PPase_dom"}]},{"database":"InterPro","id":"IPR022310","properties":[{"key":"EntryName","value":"NAD/GMP_synthase"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF000848","properties":[{"key":"EntryName","value":"guaA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00884","properties":[{"key":"EntryName","value":"guaA_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00888","properties":[{"key":"EntryName","value":"guaA_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922:SF2","properties":[{"key":"EntryName","value":"GMP SYNTHASE [GLUTAMINE-HYDROLYZING]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922","properties":[{"key":"EntryName","value":"GMP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00958","properties":[{"key":"EntryName","value":"GMP_synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02540","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54810","properties":[{"key":"EntryName","value":"GMP synthetase C-terminal dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51553","properties":[{"key":"EntryName","value":"GMPS_ATP_PPASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQQHNVLILDFGSQYTQLIARRVRELNIYCEIHPYNKIPQNLNDFKAVILSGSPSSVRSEEAPHPDLSEIRGKKPLLAVCYGAQYLAHFSGGLVAPSNTREYGRANLSFIKEDEEFFKGISQGSQVWMSHSDTIKELPTGGTLLASTHDVENAAYKIEGETTYAIQFHPEVYHSTDGKQLLQNFLVTIAGVAQTWTPDSFVDETVAELKAKIGDDKVVLGLSGGVDSTVAAVLLHKAIGSNLHCIFVNNGLLRKNEFTDVLKQYEGMGLNVKGVDASARFLGELAGLSDPEAKRKAIGKVFIDVFDDEAHQIEDAKWLAQGTIYPDVIESVSVNGGPSATIKSHHNVGGLPDFMKLKVVEPLRMIFKDEVRRVGASMGIDKELLGRHPFPGPGLAIRILGDITAEKVRILQEVDAVFINGLKESGLYDKVWQAGAILLPVNSVGVMGDERTYEKVVALRAVESTDGMTADWVNLPYEFLQKTSNKIINNVKGVNRVVYDISSKPPATIEWE","length":511,"molWeight":56130,"crc64":"9A6F78E21F8DCEAF","md5":"1E87868873AB1951933CD69D1289206A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":3,"Binding site":1},"uniParcId":"UPI000E7323A0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYC9","uniProtkbId":"A0A420DYC9_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02844.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Pyridoxine/pyridoxamine 5'-phosphate oxidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"1.4.3.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"PNP/PMP oxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"PNPOx"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Pyridoxal 5'-phosphate synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"pdxH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02844.1"}],"value":"C8N26_2484"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pyridoxamine 5'-phosphate + O2 + H2O = pyridoxal 5'-phosphate + H2O2 + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15817"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:58451"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"1.4.3.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15149"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:58589"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"1.4.3.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"value":"Binds 1 FMN per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007301"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Belongs to the pyridoxamine 5'-phosphate oxidase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02844.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"Pyridoxamine 5'-phosphate oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01243"}]},{"type":"Domain","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"Pyridoxine 5'-phosphate oxidase dimerisation C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10590"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000190-2"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01629"}],"id":"KW-0664","category":"Biological process","name":"Pyridoxine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02844.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02844.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000012","properties":[{"key":"ProteinId","value":"RKF02844.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187528.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000012.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYC9","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA01068","properties":[{"key":"RectionId","value":"UER00304"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004733","properties":[{"key":"GoTerm","value":"F:pyridoxamine phosphate oxidase 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":"Gene3D","id":"2.30.110.10","properties":[{"key":"EntryName","value":"Electron Transport, Fmn-binding Protein, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01629","properties":[{"key":"EntryName","value":"PdxH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000659","properties":[{"key":"EntryName","value":"Pyridox_Oxase"}]},{"database":"InterPro","id":"IPR019740","properties":[{"key":"EntryName","value":"Pyridox_Oxase_CS"}]},{"database":"InterPro","id":"IPR011576","properties":[{"key":"EntryName","value":"Pyridox_Oxase_N"}]},{"database":"InterPro","id":"IPR019576","properties":[{"key":"EntryName","value":"Pyridoxamine_oxidase_dimer_C"}]},{"database":"InterPro","id":"IPR012349","properties":[{"key":"EntryName","value":"Split_barrel_FMN-bd"}]},{"database":"NCBIfam","id":"TIGR00558","properties":[{"key":"EntryName","value":"pdxH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004231","properties":[{"key":"EntryName","value":"PRK05679.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10851:SF0","properties":[{"key":"EntryName","value":"PYRIDOXINE-5'-PHOSPHATE OXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10851","properties":[{"key":"EntryName","value":"PYRIDOXINE-5-PHOSPHATE OXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10590","properties":[{"key":"EntryName","value":"PNP_phzG_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01243","properties":[{"key":"EntryName","value":"PNPOx_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000190","properties":[{"key":"EntryName","value":"Pyd_amn-ph_oxd"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50475","properties":[{"key":"EntryName","value":"FMN-binding split barrel"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01064","properties":[{"key":"EntryName","value":"PYRIDOX_OXIDASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAHDLSDYRKSYEKRELLEDNCPENPIELFRDWFFTADESELVDEANAMTIASIGLDGFPKSRVVLLKKYTWEGFIFYTNYNSEKGKAILNNNHVCLSFFWSSLEQQIIIKGKAEKLAENLSDGYFESRPDGSKLGAWASNQSEVVTSRNELDNNLASFERKFENQDIPRPKHWGGFLVKPVSIEFWQGRPNRMHDRIRYTLQKDFSWKLERLAP","length":215,"molWeight":25142,"crc64":"C1386C94DC2BCBC3","md5":"DB067B2BE48A953C3D587D5AFE8FCFA1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":13},"uniParcId":"UPI000E72B937"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYD2","uniProtkbId":"A0A420DYD2_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2019-05-08","entryVersion":15,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02803.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019595"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"dTDP-4-dehydrorhamnose 3,5-epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012098"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"5.1.3.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"Thymidine diphospho-4-keto-rhamnose 3,5-epimerase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02803.1"}],"value":"C8N26_2651"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001997"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16969"},{"database":"ChEBI","id":"CHEBI:57649"},{"database":"ChEBI","id":"CHEBI:62830"}],"ecNumber":"5.1.3.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001298"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"value":"Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02803.1"}],"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":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-1"}]},{"type":"Active site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-1"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600888-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364069"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02803.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02803.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02803.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187633.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYD2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00124","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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:0008830","properties":[{"key":"GoTerm","value":"F:dTDP-4-dehydrorhamnose 3,5-epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019305","properties":[{"key":"GoTerm","value":"P:dTDP-rhamnose biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000271","properties":[{"key":"GoTerm","value":"P:polysaccharide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00438","properties":[{"key":"EntryName","value":"cupin_RmlC"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000888","properties":[{"key":"EntryName","value":"RmlC-like"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"NCBIfam","id":"TIGR01221","properties":[{"key":"EntryName","value":"rmlC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21047","properties":[{"key":"EntryName","value":"DTDP-6-DEOXY-D-GLUCOSE-3,5 EPIMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21047:SF2","properties":[{"key":"EntryName","value":"THYMIDINE DIPHOSPHO-4-KETO-RHAMNOSE 3,5-EPIMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00908","properties":[{"key":"EntryName","value":"dTDP_sugar_isom"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFIKTAIPEVVIIEPKVFGDYRGYFFESYNQKEFEENIGKINFVQDNESKSSFGVLRGLHFQKPPYTQAKLVRCIKGKVLDVAVDIRKKSPTYGKYVVVELSEENKRQLFVPRGFAHGFVVVSDEAIFSYKVDNRYAPEYDAGIAWNDSMLNIDWTISESEVRLSEKDQKLPMLEELENPFI","length":183,"molWeight":21191,"crc64":"841CFA1B0E21AC74","md5":"D75875A6F7D82DA9B759E0830431CF40"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":2,"Binding site":8,"Site":1},"uniParcId":"UPI000E74DD3E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYE4","uniProtkbId":"A0A420DYE4_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02831.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridine synthase A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"5.4.99.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridine(38-40) synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridylate synthase I"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA-uridine isomerase I"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"truA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02831.1"}],"value":"C8N26_2681"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22376"},{"database":"Rhea","id":"RHEA-COMP:10085"},{"database":"Rhea","id":"RHEA-COMP:10087"},{"database":"ChEBI","id":"CHEBI:65314"},{"database":"ChEBI","id":"CHEBI:65315"}],"ecNumber":"5.4.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003792"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009375"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003792"}],"value":"Belongs to the tRNA pseudouridine synthase TruA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02831.1"}],"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":149,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Pseudouridine synthase I TruA alpha/beta","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01416"}]},{"type":"Active site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001430-1"}]},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001430-2"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02831.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02831.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02831.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187658.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYE4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0160147","properties":[{"key":"GoTerm","value":"F:tRNA pseudouridine(38-40) synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0031119","properties":[{"key":"GoTerm","value":"P:tRNA pseudouridine synthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.70.660","properties":[{"key":"EntryName","value":"Pseudouridine synthase I, catalytic domain, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.580","properties":[{"key":"EntryName","value":"Pseudouridine synthase I, catalytic domain, N-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00171","properties":[{"key":"EntryName","value":"TruA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020103","properties":[{"key":"EntryName","value":"PsdUridine_synth_cat_dom_sf"}]},{"database":"InterPro","id":"IPR001406","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA"}]},{"database":"InterPro","id":"IPR020097","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA_a/b_dom"}]},{"database":"InterPro","id":"IPR020095","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA_C"}]},{"database":"InterPro","id":"IPR020094","properties":[{"key":"EntryName","value":"TruA/RsuA/RluB/E/F_N"}]},{"database":"PANTHER","id":"PTHR11142","properties":[{"key":"EntryName","value":"PSEUDOURIDYLATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11142:SF0","properties":[{"key":"EntryName","value":"TRNA PSEUDOURIDINE SYNTHASE-LIKE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01416","properties":[{"key":"EntryName","value":"PseudoU_synth_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001430","properties":[{"key":"EntryName","value":"tRNA_psdUrid_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55120","properties":[{"key":"EntryName","value":"Pseudouridine synthase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNYKYAYLVRFQYLGFRLHGWQKQPNLKTVHFFVDKTLKFVCKGIRCKSVGVGRTDAKVSSTDYYFQLFIDEKLDEPFFMEDFNRNSPSDIRVVAVEQLHDESFNIIQHPKTKEYRYYFSYGEKNHPYCAAFLTGYLEELDVELMKQGAQLFQGNHNFKHYCTKPSPETKVEREIDVCKIEENTELTASFFPEKSYVLIIRGSGFLRNQIRLIMGALAELGKGNYDLEFIKRSLSPENSNIDFMKTIAPASGLHLHKVEFKK","length":262,"molWeight":30657,"crc64":"7E52E9511B1149C9","md5":"E62C40D09D809ADDDC303DB0C0874FEF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":1},"uniParcId":"UPI000E757F63"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYE8","uniProtkbId":"A0A420DYE8_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02797.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018266"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"Cytidine deaminase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012783"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"3.5.4.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032005"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"Cytidine aminohydrolase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02797.1"}],"value":"C8N26_2645"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2'-deoxycytidine + H2O + H(+) = 2'-deoxyuridine + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13433"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15698"},{"database":"ChEBI","id":"CHEBI:16450"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.4.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049252"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine + H2O + H(+) = uridine + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16069"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17562"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.4.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049558"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006576"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"Belongs to the cytidine and deoxycytidylate deaminase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02797.1"}],"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":21,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"CMP/dCMP-type deaminase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51747"}]},{"type":"Active site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-1"}]},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02797.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02797.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02797.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187628.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYE8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","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:0004126","properties":[{"key":"GoTerm","value":"F:cytidine deaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:1901135","properties":[{"key":"GoTerm","value":"P:carbohydrate derivative metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0055086","properties":[{"key":"GoTerm","value":"P:nucleobase-containing small molecule metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0072527","properties":[{"key":"GoTerm","value":"P:pyrimidine-containing compound metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01283","properties":[{"key":"EntryName","value":"cytidine_deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.140.10","properties":[{"key":"EntryName","value":"Cytidine Deaminase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016192","properties":[{"key":"EntryName","value":"APOBEC/CMP_deaminase_Zn-bd"}]},{"database":"InterPro","id":"IPR002125","properties":[{"key":"EntryName","value":"CMP_dCMP_dom"}]},{"database":"InterPro","id":"IPR050202","properties":[{"key":"EntryName","value":"Cyt/Deoxycyt_deaminase"}]},{"database":"InterPro","id":"IPR006262","properties":[{"key":"EntryName","value":"Cyt_deam_tetra"}]},{"database":"InterPro","id":"IPR016193","properties":[{"key":"EntryName","value":"Cytidine_deaminase-like"}]},{"database":"NCBIfam","id":"TIGR01354","properties":[{"key":"EntryName","value":"cyt_deam_tetra"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004064","properties":[{"key":"EntryName","value":"PRK05578.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11644","properties":[{"key":"EntryName","value":"CYTIDINE DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11644:SF2","properties":[{"key":"EntryName","value":"CYTIDINE DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00383","properties":[{"key":"EntryName","value":"dCMP_cyt_deam_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53927","properties":[{"key":"EntryName","value":"Cytidine deaminase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00903","properties":[{"key":"EntryName","value":"CYT_DCMP_DEAMINASES_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51747","properties":[{"key":"EntryName","value":"CYT_DCMP_DEAMINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKINVTTSAIVFDNISQLSPEDAFLLEKAVEARQKAYAPYSKFNVGAAILLDNGEVVLGNNQESAAYPSGMCAERVAIWKAGSEYPTMKVLKIAITASSENSKVDKPVGPCGACRQTLSEYEINQKQPIEILFMGEVGQIVKTESLLSLLPFSFDSSYL","length":160,"molWeight":17417,"crc64":"F01AE56BCA600824","md5":"89B02F41F99853BDE4DDF9F3F8874864"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":4},"uniParcId":"UPI000E73785B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYF1","uniProtkbId":"A0A420DYF1_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02823.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019357"}],"value":"Dihydrofolate synthase/folylpolyglutamate synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013023"}],"value":"6.3.2.12"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013025"}],"value":"6.3.2.17"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032510"}],"value":"Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030048"}],"value":"Folylpolyglutamate synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030592"}],"value":"Tetrahydrofolylpolyglutamate synthase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02823.1"}],"value":"C8N26_2673"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002714"}],"value":"Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51912"},{"database":"Rhea","id":"RHEA-COMP:13257"},{"database":"Rhea","id":"RHEA-COMP:13258"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:136572"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049035"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10580"},{"database":"Rhea","id":"RHEA-COMP:14738"},{"database":"Rhea","id":"RHEA-COMP:14740"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:141005"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047493"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51904"},{"database":"Rhea","id":"RHEA-COMP:13088"},{"database":"Rhea","id":"RHEA-COMP:14300"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:134413"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047808"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7,8-dihydropteroate + L-glutamate + ATP = 7,8-dihydrofolate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23584"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17839"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57451"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049161"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004799"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005150"}],"value":"Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008276"}],"value":"Belongs to the folylpolyglutamate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02823.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022909"}],"id":"KW-0289","category":"Biological process","name":"Folate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02823.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02823.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000013","properties":[{"key":"ProteinId","value":"RKF02823.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187652.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000013.1"}]},{"database":"AlphaFoldDB","id":"A0A420DYF1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008841","properties":[{"key":"GoTerm","value":"F:dihydrofolate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004326","properties":[{"key":"GoTerm","value":"F:tetrahydrofolylpolyglutamate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"3.40.1190.10:FF:000011","properties":[{"key":"EntryName","value":"Folylpolyglutamate synthase/dihydrofolate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001645","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth"}]},{"database":"InterPro","id":"IPR018109","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth_CS"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"NCBIfam","id":"TIGR01499","properties":[{"key":"EntryName","value":"folC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11136:SF0","properties":[{"key":"EntryName","value":"DIHYDROFOLATE SYNTHETASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11136","properties":[{"key":"EntryName","value":"FOLYLPOLYGLUTAMATE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001563","properties":[{"key":"EntryName","value":"Folylpolyglu_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01011","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01012","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTYQEILDWMFAQLPMYQRQGKTAFKKDLTNIIALCDELDNPQKKFKTIHVGGTNGKGSTSHMVASILQEAGYKVGLYTSPHLKNFTERIRVNGEEISREAVIEFIEKNKNFLENQGLSFFEMTVGMAFKEFANQNVDIAVIEVGLGGRLDSTNIITPEVSVITNIGLDHTQFLGETLPEIAFEKAGIIKYGVPVVIGEHQKETESVFTAKAEECKAPIVFASDNPKNYTTDLLGDYQKNNVTTAVTAIQRLKGFSISEENIKNGLLNVVKNTNLKGRWQVLQNNPKVICDTAHNKEGLFYTLKQLKKENYKQLHMVLGVVSDKNLSEILPMFPKNAMYYFCKPNIPRGLSADELKEQAKEFGLVGKVFCSVSQALEKSKENAAKEDVIYIGGSTFVVAEIL","length":402,"molWeight":44911,"crc64":"A233E57FD0C0C131","md5":"5AADF298B88FD4870521778C6C2B89AC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI000E7607F8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A420DYK8","uniProtkbId":"A0A420DYK8_9FLAO","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Tenacibaculum lutimaris","taxonId":285258,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02882.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Tenacibaculum"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"DNA-directed RNA polymerase subunit beta'"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"RNAP subunit beta'"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"RNA polymerase subunit beta'"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"Transcriptase subunit beta'"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"rpoC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02882.1"}],"value":"C8N26_2524"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004279"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004279"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"value":"The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004279"}],"value":"Belongs to the RNA polymerase beta' chain family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02882.1"}],"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":252,"modifier":"EXACT"},"end":{"value":531,"modifier":"EXACT"}},"description":"RNA polymerase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00663"}]},{"type":"Region","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":824,"modifier":"EXACT"},"end":{"value":824,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":898,"modifier":"EXACT"},"end":{"value":898,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":905,"modifier":"EXACT"},"end":{"value":905,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":908,"modifier":"EXACT"},"end":{"value":908,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022478"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01322"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-5I363GG4TU291","citationType":"submission","authors":["Goeker M."],"title":"Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II (KMG-II): from individual species to whole genera.","publicationDate":"SEP-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02882.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}],"value":"DSM 16505","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RKF02882.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000285780"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"RAQM01000012","properties":[{"key":"ProteinId","value":"RKF02882.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_120187554.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_RAQM01000012.1"}]},{"database":"Proteomes","id":"UP000285780","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase 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:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02655","properties":[{"key":"EntryName","value":"RNAP_beta'_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01609","properties":[{"key":"EntryName","value":"RNAP_beta'_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.132.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.390","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1790.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.40.90","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.40.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"3.30.60.280","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"4.10.860.120","properties":[{"key":"EntryName","value":"RNA polymerase II, clamp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.274.100","properties":[{"key":"EntryName","value":"RNA polymerase Rpb1, domain 3"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01322","properties":[{"key":"EntryName","value":"RNApol_bact_RpoC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045867","properties":[{"key":"EntryName","value":"DNA-dir_RpoC_beta_prime"}]},{"database":"InterPro","id":"IPR012754","properties":[{"key":"EntryName","value":"DNA-dir_RpoC_beta_prime_bact"}]},{"database":"InterPro","id":"IPR000722","properties":[{"key":"EntryName","value":"RNA_pol_asu"}]},{"database":"InterPro","id":"IPR006592","properties":[{"key":"EntryName","value":"RNA_pol_N"}]},{"database":"InterPro","id":"IPR007080","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_1"}]},{"database":"InterPro","id":"IPR007066","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_3"}]},{"database":"InterPro","id":"IPR042102","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_3_sf"}]},{"database":"InterPro","id":"IPR007083","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_4"}]},{"database":"InterPro","id":"IPR007081","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_5"}]},{"database":"InterPro","id":"IPR044893","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_clamp_domain"}]},{"database":"InterPro","id":"IPR038120","properties":[{"key":"EntryName","value":"Rpb1_funnel_sf"}]},{"database":"NCBIfam","id":"TIGR02386","properties":[{"key":"EntryName","value":"rpoC_TIGR"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19376","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19376:SF54","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04997","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00623","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF04983","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05000","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04998","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_5"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00663","properties":[{"key":"EntryName","value":"RPOLA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64484","properties":[{"key":"EntryName","value":"beta and beta-prime subunits of DNA dependent RNA-polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARKNEKYTVKKFNKISIGLASPESILEASKGEVLKPETINYRTHKPERDGLFCERIFGPVKDYECACGKYKRIRYKGIVCDRCGVEVTEKKVRRDRVGHINLVVPVAHIWYFRSLPNKMGYLLGLPSKKLDMIIYYERYVVIQPGIAKNAEGEPLQKMDFLTEEEYLDILDTLPQENMYLEDTDPNKFIAKMGAECLIDLLERIDLDQLSYELRHKANTETSKQRKNEALKRLNVVEAFRDSQKNRENNPEWMIMKVIPVIPPELRPLVPLDGGRFATSDLNDLYRRVIIRNNRLKRLMEIKAPEVILRNEKRMLQESVDSLFDNTRKSSAVKTESNRPLKSLSDSLKGKQGRFRQNLLGKRVDYSARSVIVVGPELRLFECGLPKDMAAELYKPFVIRKLIERGIVKTVKSAKKIIDRKEPVVWDILENVIKGHPVLLNRAPTLHRLGIQAFQPKLIEGKAIRLHPLACSAFNADFDGDQMAVHLPLGPEAILEAQLLMLGSHNILNPANGAPITVPSQDMVLGLYYMTKERKSTPEVPIKGEGLTFYSPEEVIIALNEEKVDLNAGIKVRTEDVENGERVVRIIETTVGRVLFNEVVPEEAGFINEVLTKKSLRGVISRILKVTDIPAVGKFLDEIKNMGYKYAFEGGLSFSLGDIIIPEEKHAMIAEANQEVDGIIMNYNMGMLTQKERYNQVIDVWGSTNNRLTELSMKRLREDQQGFNSVFMMLDSGARGSKEQIRQLTGMRGLMAKPKKSTASGGEIIENPILSNFKEGLSILEYFISTHGARKGLADTALKTADAGYLTRRLVDVSQDVIINEVDCGTLRGLEVSPLKKNDEIVESLSDRISGRTALHDVYPPNSDELLIAAGELITPLLADKIEAAGVDTVEVRSALTCESEKGICEKCYGQSMSTGQKVQRGEAVGVIAAQSIGEPGTQLTLRTFHVGGVAGNISEDNKLIAKFDGNVTIDDLRTVKGKDAAGEEVDIVISRTAEIKIIDKKNGVVLSTNIIPYGSIIFDKDRETIKKGDAVCQWDPFNGVIVSEFAGKVKFDNLEQGINYSVEIDEQTGFQEKVITDSKNKKIIPSLIIEDADGNALRSYSLPVGAHLIVDNGDKVESGKTLVKIPRKSGKAGDITGGLPRVTELFEARNPSNPAVVAEIDGVVSFGKIKRGNREIIIESKTGDVRKYLIKLSNQILVQENDFIKAGMPLSDGAITPTDILNIKGPSAVQEYLVNEIQEVYRLQGVKINDKHFEVVVRQMMRKVRIIDSGDTLFLENQLVHKTDFIKENDAIYGMKVVEDSGDSANLKPGQIVSARQLRDENSLLRREDKNLVIARDAQPATAEQVLQGITRASLQTKSFISAASFQETTKVLNEAAVNGKVDTLEGLKENVIVGKRIPAGTGMRSYDDLIVGPKDEIEQSL","length":1423,"molWeight":158505,"crc64":"F1CF7108C8E457EC","md5":"34B76F4772538194D913ABEB8D6AA4C5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":11},"uniParcId":"UPI000E732CA3"}}]}