{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HVT4","uniProtkbId":"A0AAE9HVT4_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10065.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10065.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10065.1"}],"value":"FGG12_24140"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) 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":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10065.1"}],"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":24,"modifier":"EXACT"},"end":{"value":1082,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5048514928"},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":683,"modifier":"EXACT"},"end":{"value":878,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":945,"modifier":"EXACT"},"end":{"value":1082,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":945,"modifier":"EXACT"},"end":{"value":1082,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":719,"modifier":"EXACT"},"end":{"value":719,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":758,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":760,"modifier":"EXACT"},"end":{"value":760,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":765,"modifier":"EXACT"},"end":{"value":765,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":790,"modifier":"EXACT"},"end":{"value":790,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":791,"modifier":"EXACT"},"end":{"value":791,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":792,"modifier":"EXACT"},"end":{"value":792,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":793,"modifier":"EXACT"},"end":{"value":793,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":833,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":833,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":833,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Binding site","location":{"start":{"value":851,"modifier":"EXACT"},"end":{"value":851,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":851,"modifier":"EXACT"},"end":{"value":851,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10065.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10065.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000018","properties":[{"key":"ProteinId","value":"TSP10065.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144201767.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000040.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HVT4","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_10745","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRTDIKSILIIGAGPIIIGQACEFDYSGAQACKALREEGYKVILVNSNPATIMTDPNTADVTYIEPITWEVVERIIERERPDAILPTMGGQTALNCALDLHRHGVLDKYKVELIGASPEAIDKAEDRQKFKDAMTKIGLGSAKSGIAHSMDEAVAVQSRIAADTGTTGYPIVIRPSFTLGGSGGGIAYNREEFEEICKRGLDLSPTRELLIEESLLGWKEYEMEVVRDKADNCIIICSIENLDPMGIHTGDSITVAPAQTLTDKEYQILRNASLAVLREIGVDTGGSNVQFSINPADGRMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELKNEITGGQTPASFEPSIDYVVTKVPRFAFEKFPQADSHLTTQMKSVGEVMAMGRTFQESFQKALRGLEVGVDGLDEKSTDRDEVVEEIGEAGPDRIWYVGDAFRLGMSLEEVHAETAIDPWFLAQIEDIVKTESIVRNRTLASLSTPELRLLKQKGFSDRRLAKLLKTDAKSVREARIAQNVRPVYKRVDTCAAEFATNTAYMYGTYEAEHGECEAEPTANKKIMVLGGGPNRIGQGIEFDYCCVHAALALREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDKEKPVGVIVQYGGQTPLKLALDLEANGVPIIGTSPDMIDAAEDRERFQKLLQELGLRQPPNRTARAEDEALRLAEEIGYPLVVRPSYVLGGRAMEIVHEPRDLERYMREAVKVSHDSPVLLDRFLNDAIECDVDALSDGQRVFIGGVMEHIEQAGVHSGDSACSLPPYSLSQATVDELKRQTAAMAKALNVIGLMNVQFAIQQHNGEDTVYVLEVNPRASRTVPYVSKATGLSLAKIAARCMAGQSLDSQGIGEEVVPPYFSVKEAVFPFNKFPGVDPVLGPEMRSTGEVMGVGKVFGEALFKSQLAAGSRLPEKGTVLITVKDSDKPRAVGVARMLHDLGYPIVATRGTASAIEAAGIPVRVVNKVKDGRPHIVDMIKNGELALVFTTVDETRTAIADSRSIRIAALAGRVPYYTTIAGARAAVEGLKHMQSLEVYDLQSLHKQLA","length":1082,"molWeight":117996,"crc64":"0CA6D8B5CAA340A0","md5":"650B340315A78EF415E0EDFE18104B97"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":3,"Region":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI00118401EB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HY64","uniProtkbId":"A0AAE9HY64_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09774.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Pyrimidine/purine nucleoside phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Adenosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Cytidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Guanosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Inosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Thymidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Uridine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Xanthosine phosphorylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"ppnP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09774.1"}],"value":"FGG12_25845"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19805"},{"database":"ChEBI","id":"CHEBI:26386"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"},{"database":"ChEBI","id":"CHEBI:142355"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27642"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine + phosphate = cytosine + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:52540"},{"database":"ChEBI","id":"CHEBI:16040"},{"database":"ChEBI","id":"CHEBI:17562"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13233"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:16750"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27646"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"thymidine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + thymine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16037"},{"database":"ChEBI","id":"CHEBI:17748"},{"database":"ChEBI","id":"CHEBI:17821"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57259"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine + phosphate = alpha-D-ribose 1-phosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24388"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"xanthosine + phosphate = alpha-D-ribose 1-phosphate + xanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27638"},{"database":"ChEBI","id":"CHEBI:17712"},{"database":"ChEBI","id":"CHEBI:18107"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Belongs to the nucleoside phosphorylase PpnP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09774.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_01537"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09774.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09774.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000021","properties":[{"key":"ProteinId","value":"TSP09774.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144202423.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000032.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HY64","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_13865","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0004731","properties":[{"key":"GoTerm","value":"F:purine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016154","properties":[{"key":"GoTerm","value":"F:pyrimidine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd20296","properties":[{"key":"EntryName","value":"cupin_PpnP-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01537","properties":[{"key":"EntryName","value":"Nucleos_phosphorylase_PpnP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009664","properties":[{"key":"EntryName","value":"Ppnp"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"PANTHER","id":"PTHR36540","properties":[{"key":"EntryName","value":"PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36540:SF1","properties":[{"key":"EntryName","value":"PYRIMIDINE_PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06865","properties":[{"key":"EntryName","value":"Ppnp"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQFDNVSVVKKANLYFDGKCVSHTVVFPDGTRKTLGVIFPATLNFNTGAPEIMEINGGSCRVRLAGSEEWKTYGAGQQFDVPGNSNFDIEVTETLDYVCHFG","length":103,"molWeight":11287,"crc64":"9945684F7B4B5CDE","md5":"BDF58D0142A504A10EBB10EC5022E17E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"SIMILARITY":1,"CAUTION":1},"uniParcId":"UPI000FA5F120"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HZD0","uniProtkbId":"A0AAE9HZD0_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09759.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09759.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09759.1"}],"value":"FGG12_25765"}]}],"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":"TSP09759.1"}],"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":18,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Coenzyme A biosynthesis bifunctional protein CoaBC","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5048514946"},{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"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":288,"modifier":"EXACT"},"end":{"value":288,"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":306,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Lipidation","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"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":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"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:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09759.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09759.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000021","properties":[{"key":"ProteinId","value":"TSP09759.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144202393.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000032.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HZD0","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_13785","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDLRGKHIVLGLTGGIACYKSAELVRLLTKAGATVQVAMTEAATHFITPVTMQALSGRPVFLSQWDARIDNNMAHIDLSREADAILIAPASTDFLAKLANGLCDDLLTTLCIARECPLLVAPAMNRQMWAAAPTQRNAAQLRADGVAILGPGTGDQACGEIGDGRMLEPAEIVEDLVAFFQPKPLAGKRVLITAGPTFEAIDPVRGITNLSSGKMGFSIARAAREAGADVLLVAGPTALPTPRGVVRTDVRSAQQMHDTVMAQLRDVDVFVAVAAVADWRPAEVSRQKLKKANDTDTPTLQFVQNPDILAAVAARADAPYCVGFAAESENLEQYGEQKRQRKGVPLLVGNIGHHTFGMDDNEIVLFDAGGMTRLPRADKLSLARDLVAAIGQRLPRKPV","length":399,"molWeight":42566,"crc64":"335006A7BFB780E9","md5":"64D2EE884B4BB224FCB921FC74CF124A"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":2,"Region":2,"Active site":1,"Binding site":6,"Lipidation":2},"uniParcId":"UPI000F9204A0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9I527","uniProtkbId":"A0AAE9I527_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14691.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"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":"TSP14691.1"}],"value":"FGG12_03385"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"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":"TSP14691.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":539,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":520,"modifier":"EXACT"},"end":{"value":520,"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":522,"modifier":"EXACT"},"end":{"value":522,"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":13,"modifier":"EXACT"},"end":{"value":13,"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":13,"modifier":"EXACT"},"end":{"value":13,"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":14,"modifier":"EXACT"},"end":{"value":19,"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":71,"modifier":"EXACT"},"end":{"value":71,"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":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":196,"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":191,"modifier":"EXACT"},"end":{"value":196,"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":227,"modifier":"EXACT"},"end":{"value":227,"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":227,"modifier":"EXACT"},"end":{"value":227,"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":245,"modifier":"EXACT"},"end":{"value":245,"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":356,"modifier":"EXACT"},"end":{"value":356,"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":384,"modifier":"EXACT"},"end":{"value":387,"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":407,"modifier":"EXACT"},"end":{"value":407,"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":473,"modifier":"EXACT"},"end":{"value":473,"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":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14691.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14691.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000001","properties":[{"key":"ProteinId","value":"TSP14691.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144196052.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000007.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9I527","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_05225","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKFVFVTGGVVSSLGKGIAAASLAAILESRGLKVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFVSAKMRKSNNFTTGQIYESVIRKERRGEYLGKTVQVIPHITNEIQAFVERGAAASHEGKADVALVEIGGTVGDIESLPFLEAARQMSLRMGRNHCAFVHLTLVPFIASAGELKTKPTQHSVQKLREIGISPTALLCRADRPIPDDERAKISLFANIPQEAVISVWDADSIYKIPQMLNEQGLDRLICEELRLDPKPADLSMWQKLVNAQENPEHEITIGMVGKYVDLTESYKSLIEALRHAGMHTATRVNIEYIDSEELESGHLEVLQPLDAILVPGGFGKRGTEGKIRAIQYARENKVPYLGICLGMQLAVIEFARHVANMADANSTEFNLETEHPVVALITEWLDREGKVEQRSADSDLGGTMRLGAQRVPVKAGTKAAQIYGDEVNERHRHRYEVNNHYVPQLEGAGMVISARTPTENLPEMMELPESLHPWFVGVQFHPEFTSTPRDGHPLFKAYVEAALASQQRKGKSA","length":552,"molWeight":61059,"crc64":"4F470388CDA42A37","md5":"8A0BADC44126B642D1C31384E013EC6C"},"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":16},"uniParcId":"UPI001182AEBA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9L0J0","uniProtkbId":"A0AAE9L0J0_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10723.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10723.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10723.1"}],"value":"FGG12_21795"}]}],"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. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"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":"TSP10723.1"}],"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":99,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"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":117,"modifier":"EXACT"},"end":{"value":117,"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":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":171,"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":202,"modifier":"EXACT"},"end":{"value":202,"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":224,"modifier":"EXACT"},"end":{"value":226,"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":301,"modifier":"EXACT"},"end":{"value":301,"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":"UP000318943"}],"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-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10723.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10723.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000014","properties":[{"key":"ProteinId","value":"TSP10723.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144200881.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000055.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9L0J0","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_10055","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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":"1.10.150.530:FF:000003","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000008","properties":[{"key":"EntryName","value":"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":"MNPLVNLLDLDADALTAYCGELGEKPFRARQLQRWIHQFGASQFDAMSDLAKSLREKLATRAEIRSPAIITDNVSADGTRKWLLDVGAGNAVETVYIPEDTRGTLCVSSQAGCAVNCRFCSTGKQGFSRNLSTGEIIGQLWMAEFAMRAQLGRGPKDDRVISNVVMMGMGEPLLNYDAVVPAMRLMLDDNAYGLSRRRVTLSTSGVVPMMDRLSKDLPVALAVSLHASNDALRDVLVPLNKKYPLAELMAACRRYLEFAPRDFITFEYCMLDGVNDGVEHARELLKLVADVPCKFNLIPFNPFPESGLKRSNNEQIRRFAQVLMDAGIVTTIRKTRGDDIDAACGQLAGEVMDRTRLAERGKFGKITPLVPVVAAGPSREARPA","length":384,"molWeight":42199,"crc64":"FDFE6F649E2F835F","md5":"7E509404A532EE1C2533DC61D7C5FB7F"},"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":"UPI000FB28964"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9L349","uniProtkbId":"A0AAE9L349_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14401.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein nucleotidyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein adenylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.108"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein uridylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"ydiU"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"selO"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14401.1"}],"value":"FGG12_01700"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Nucleotidyltransferase involved in the post-translational modification of proteins. It can catalyze the addition of adenosine monophosphate (AMP) or uridine monophosphate (UMP) to a protein, resulting in modifications known as AMPylation and UMPylation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-[protein] + UTP = N(tele)-(5'-uridylyl)-L-histidyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83891"},{"database":"Rhea","id":"RHEA-COMP:9745"},{"database":"Rhea","id":"RHEA-COMP:20239"},{"database":"ChEBI","id":"CHEBI:29979"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:233474"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58120"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:15073"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:142516"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + UTP = O-(5'-uridylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64604"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:16635"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:156051"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54292"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:13847"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:138113"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-(5'-adenylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54288"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:13846"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + UTP = O-(5'-uridylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83887"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20238"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:90602"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009747"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Belongs to the SELO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14401.1"}],"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":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"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_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_00692"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14401.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14401.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000001","properties":[{"key":"ProteinId","value":"TSP14401.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144195566.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000023.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9L349","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_07120","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0070733","properties":[{"key":"GoTerm","value":"F:AMPylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_00692","properties":[{"key":"EntryName","value":"YdiU_SelO"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003846","properties":[{"key":"EntryName","value":"SelO"}]},{"database":"NCBIfam","id":"NF000658","properties":[{"key":"EntryName","value":"PRK00029.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057:SF14","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02696","properties":[{"key":"EntryName","value":"SelO"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPESPVPFRTAPGFAALGERFFTRLQPTPLPSPYLVSVAPAAAALLGWSPQTIGAEASQPDFLDTFIGNRVPDWADPLATVYSGHQFGVWAGQLGDGRAIRLAEAERDDGPWEIQLKGGGLTPYSRMADGRAVLRSSIREYLCSEAMYALGVPTTRALAIVGSDAPVRRETIETAAVVTRLAPSFIRFGHFEHFAAREDHAALRELADFVIDRFYPACRDAGGNPYQALLREVSLRTADMVAHWQAVGFCHGVMNTDNMSILGLTIDYGPFGFLDAFDANHICNHSDQQGRYAYSQQPQVAFWNLHCLAQALLPLWRDTDAADAADPEAAKEAAVAAAREALDPFRDRYAAAFFRHYRAKLGLRPLGGQENEDEALLTNLFRVLHANRVDYTLFWRNLARISGKDASADAPVRDLFLDRAAWDAWAAEYRARLQAEQSDDATRAAGMLAVNPKYILRNHLAETAIRAARDKDFSEVDRLLAVLSRPFDEQPEAEAYAALPPDWASGLEVSCSS","length":514,"molWeight":56610,"crc64":"10C388182953B640","md5":"0A0EC169AC221280180558628C4314FA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":11},"uniParcId":"UPI000F9FC9E8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9L3F6","uniProtkbId":"A0AAE9L3F6_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14418.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"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_01965"}],"value":"nnrD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14418.1"}],"value":"FGG12_01790"}]}],"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":"TSP14418.1"}],"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":39,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":533,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":88,"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":85,"modifier":"EXACT"},"end":{"value":85,"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":158,"modifier":"EXACT"},"end":{"value":158,"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":162,"modifier":"EXACT"},"end":{"value":168,"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":191,"modifier":"EXACT"},"end":{"value":191,"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":194,"modifier":"EXACT"},"end":{"value":194,"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":290,"modifier":"EXACT"},"end":{"value":290,"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":346,"modifier":"EXACT"},"end":{"value":346,"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":405,"modifier":"EXACT"},"end":{"value":405,"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":442,"modifier":"EXACT"},"end":{"value":446,"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":472,"modifier":"EXACT"},"end":{"value":472,"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":473,"modifier":"EXACT"},"end":{"value":473,"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":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14418.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14418.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000001","properties":[{"key":"ProteinId","value":"TSP14418.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144195601.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000023.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9L3F6","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_07025","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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":"MTASPSPSSASSASSATHDWLPLDPTGTDATPLHDVATIREIEHAALAALPAFTLMTRAGHAAADWLAQQVPDGRIVLLAGAGNNGGDALVAATRLHQSGRQVEVWLTAETDRLPPDASRAWTEARTAGVPLLAVPADPSNATAALPPWPAGCTALVDGLLGIGLNRPADGNMARWIDHVNAAGLPVYALDIPSGLFADTGAGRPAIRARRTLTFIAAKPGLLTLDGRDCAGEIDIAPLGLPYPPTQTAIAHVNLPGAFRDALPGRPHAVNKGTFGSLAVLGGSHGMAGAPLLGARAALHLGAGRVHVGFLAQPAPLMDPVHPELMLHDVADMAVETMSALVIGPGMGTGGAAGKLLGQWIDTCAKVGSPPPLVLDADALNLLAGDQTLADALRASGVPHVMTPHPLEAARLLGCTVAEIQRDRLSAARALAAAWQATIVLKGSGTLIAAAGVDSIAINPTGNAALATAGTGDVLAGMIGALLAQGMAPTDAACAAVWIHGRAADRLVSNGTGPAGMTASELYLPARAILNALTQGRAA","length":539,"molWeight":54356,"crc64":"DE535A2BDFAC7102","md5":"9E00B787A6CC467AF3D5EFF1E047BE6B"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":12},"uniParcId":"UPI001183882D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3EHX3","uniProtkbId":"A0ABY3EHX3_9BURK","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10421.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"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":"TSP10421.1"}],"value":"FGG12_22680"}]}],"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":"TSP10421.1"}],"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":333,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"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":123,"modifier":"EXACT"},"end":{"value":129,"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":165,"modifier":"EXACT"},"end":{"value":166,"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":192,"modifier":"EXACT"},"end":{"value":192,"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":198,"modifier":"EXACT"},"end":{"value":198,"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":200,"modifier":"EXACT"},"end":{"value":200,"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":407,"modifier":"EXACT"},"end":{"value":407,"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":431,"modifier":"EXACT"},"end":{"value":434,"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":482,"modifier":"EXACT"},"end":{"value":482,"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":486,"modifier":"EXACT"},"end":{"value":486,"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":232,"modifier":"EXACT"},"end":{"value":232,"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":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"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":"TSP10421.1"}],"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":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10421.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10421.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000016","properties":[{"key":"ProteinId","value":"TSP10421.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144201466.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000024.1"}]},{"database":"Proteomes","id":"UP000318943","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":"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":"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":"MTAKPLLPLEVSVQASNALAWLRTHAPVTARLTGDTRRLQPGDVFFAYVLGNDRLATDGRPHIDKAIAAGASAIVHEADGYAWTHGDAVPHLAVSQLHELAGPIAAGWHGVAARGLTVTGITGTNGKTSCAQWLARLLQATGTRCATIGTLGTGFPDALQATGFTTPDAVQLQASLADLHDAGARAIAMEVSSHGLEQGRVAGTGFAVAVLTNLTQDHLDYHGTMAEYEAAKARLFQWDGLRAAVINRDDAMGRRLLAGNAAAVTAPQVIEYGIDGAAGASAARGQWLRASGVRATASGTAFHLDGSFGSADVTTPMIGKFNVSNLLAVLGAALAQGVAWDAALAALRTLTPVDGRMELFGGQDAPLAVVDYAHTPDALAQTLAALRPVAEARQGRLWCVFGCGGDRDATKRPLMGGVAERLADDIILTSDNPRSEDPRDILEAIADGMQDRARARLVEDRAAAILYAIKHAATADVVLVAGKGHEATQEIQGKKRPFSDREHVRLTLGTRGVSA","length":515,"molWeight":53754,"crc64":"39D950E8A4F28B68","md5":"6F5939CE6FFF017C135E6CBAC2ADE6E6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI00118411F4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3ELA9","uniProtkbId":"A0ABY3ELA9_9BURK","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11660.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11660.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11660.1"}],"value":"FGG12_16345"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11660.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Domain","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"Mannose-1-phosphate guanyltransferase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF25087"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"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_01631"}],"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_01631"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11660.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11660.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000009","properties":[{"key":"ProteinId","value":"TSP11660.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144199094.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_VCIZ01000009.1"}]},{"database":"Proteomes","id":"UP000318943","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:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase 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:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"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":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR056729","properties":[{"key":"EntryName","value":"GMPPB_C"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25087","properties":[{"key":"EntryName","value":"GMPPB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNIVILAAGMGKRMNSALPKVLHPVAGRPMLAHVLDTARTLSPSRLVVVVGHGAEHVREAVGAPDVAFAEQTQQLGTGHAVMQALPLLDDSQPTLVLYGDVPLTTAATLEALVHAAGAERLGVLTVEMPDPTGYGRIVRDAAGNIVRIVEQKDASDEIRAIREINTGIIVCPTGHLRRWLATLGNDNAQGEYYLTDTIERAANEGVEIVSAQPAALWETLGVNSKVQLAEVERIHQRNLAQRLLEAGVTLPDPARIDVRGQLTCGRDVTIDVGCVFEGRVHLDDGVHISAHCVIRNATIGAGARVQPFCHIEEAKIGPAGRIGPYARLRPGTELGEDVHIGNFVEVKNSQVGDHSKANHLAYVGDSTVGQRVNIGAGTITCNYDGVNKSRTVIEDDAFIGSDTQLVAPVTVGRGATIGAGTTLTKDAPAGKLTLSRAKQMTLDAWQRPVKQPKQSK","length":456,"molWeight":48491,"crc64":"1398148A6F2485CC","md5":"4135E48EA34841E49DF59312633A6382"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI0011834E05"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3EMG0","uniProtkbId":"A0ABY3EMG0_9BURK","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate dehydrogenase [ubiquinone]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"1.2.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate oxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"POX"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate:ubiquinone-8 oxidoreductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"}],"value":"poxB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"}],"value":"FGG12_13990"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + pyruvate + H2O = a ubiquinol + acetate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27405"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:30089"}],"ecNumber":"1.2.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362132"}],"value":"Belongs to the TPP enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"}],"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":115,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00205"}]},{"type":"Domain","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":531,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]},{"type":"Region","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":578,"modifier":"EXACT"}},"description":"Membrane-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"Moves into active site upon enzyme activation, plays a role in electron transfer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12121.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000007","properties":[{"key":"ProteinId","value":"TSP12121.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144198271.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_VCIZ01000007.1"}]},{"database":"Proteomes","id":"UP000318943","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:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008289","properties":[{"key":"GoTerm","value":"F:lipid 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:0052737","properties":[{"key":"GoTerm","value":"F:pyruvate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048039","properties":[{"key":"GoTerm","value":"F:ubiquinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042867","properties":[{"key":"GoTerm","value":"P:pyruvate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02014","properties":[{"key":"EntryName","value":"TPP_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07039","properties":[{"key":"EntryName","value":"TPP_PYR_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1220:FF:000013","properties":[{"key":"EntryName","value":"Pyruvate dehydrogenase [ubiquinone]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00850","properties":[{"key":"EntryName","value":"POX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR047211","properties":[{"key":"EntryName","value":"POXB-like"}]},{"database":"InterPro","id":"IPR044261","properties":[{"key":"EntryName","value":"Pyruvate_dehydrogenase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012000","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_cen_dom"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR000399","properties":[{"key":"EntryName","value":"TPP-bd_CS"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"InterPro","id":"IPR047212","properties":[{"key":"EntryName","value":"TPP_POXB-like"}]},{"database":"InterPro","id":"IPR047210","properties":[{"key":"EntryName","value":"TPP_PYR_POXB-like"}]},{"database":"NCBIfam","id":"NF006591","properties":[{"key":"EntryName","value":"poxB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981:SF2","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00205","properties":[{"key":"EntryName","value":"TPP_enzyme_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00187","properties":[{"key":"EntryName","value":"TPP_ENZYMES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANHASDLITRVLHAVGVERIYGVVGDSLNGITESLRQRDDIDWIHTRHEETAAFAAGAEAHLTGKLAVCAGSCGPGNLHLINGLFDCHRSGVPVLAIAAHIPSAEIGRGYFQETHPEQLFRECSHYCELVTSVEQLPGVLESAIRAAVGRRGVAVIVIPGDVALREGTFAESAPAAIALRPPVVTPDAASLDALASLLRGSQRTTLLCGRGCAGAHDQVVQLAATLKAPVVHALGGKEYIEYDNPYDVGMTGLIGFSSGYHAMQECDTLLMLGTDFPYRQFYPEGAQVVQIDIRPENLGRRTRLDMGLVGDVGATLDALLPRLAPKADEADEAHLAASLRHYRDARRQLDDLATGDSGRKPIHPQYLARLLSEQAAEDAVFTFDVGTPTIWAARYLRMNGQRRLIGSLAHGSMANALPQAIGAQSAYPGRQVISLSGDGGFAMLMGDFLTLAQQGLPVKVVIVNNSVLGFVALEMKASGYLESGTSLQNPDFAAMARAIGVHAQRVEDPLLLPEAIATMLAHDGPALLDVVTNTQELAMPPSLKAEQVKGFSLWAMKAVMNGRADEVIELARSNLLR","length":578,"molWeight":61740,"crc64":"4EA0636117D70C4B","md5":"476CFE4698FA664F17696F3CA7AEEC36"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":1,"Binding site":9,"Site":1},"uniParcId":"UPI0011835E4D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3ETK5","uniProtkbId":"A0ABY3ETK5_9BURK","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14272.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14272.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14272.1"}],"value":"FGG12_01005"}]}],"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":"ARBA","id":"ARBA00051651"},{"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":"TSP14272.1"}],"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":124,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Active site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"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":283,"modifier":"EXACT"},"end":{"value":283,"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":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-90)","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":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14272.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP14272.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000001","properties":[{"key":"ProteinId","value":"TSP14272.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144195310.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000018.1"}]},{"database":"Proteomes","id":"UP000318943","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:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"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":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSYEKCPFNHAAGGGTTNKDWWPQQLRLDLLSQHSDKSNPLDKSFNYAEAFKSLDLAAVKQDLTALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRIGDGRGGGGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLMILAGNVALESMGFKTFGFAGGREDTWEPDQDVYWGNEKTWLGGDVRYGKGAAGKDDDGGVLVADVQKHGQEVSRTDPGRYLENPLGAVQMGLIYVNPEGPDGNPDPIAAAYDIRDTFGRMAMDDEETVALIAGGHSFGKTHGAAHPENVGDEPESAELELQGLGWRNKFGTGCGPDTITSGLEVTWSNTPTKWGNSFFENLFNFEYELTKSPAGANQWIAKDAPETVPHAYDPARKLKPTMLTTDLSLRFDPIYEKISRRFKDDPQAFADAFARAWFKLTHRDMGPRARYLGPEVPAEELLWQDPIPPVDHPLVNDQDVAGLKQKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWPANNPDQLGKVLKTLEGIQGEFNGAQSGGKKISMADLIVLAGSAGIEKAAEAGGQKLTVPFTPGRMDASQDKTDVESVGALEPKADGFRNYLDAKVQAPAEAMLIDKAQLLTLTAPEMTALIGGLRVLKVQSGKDAHGVLTDRPETLTNDFFRNLLDMGVQWKPVSRNVFEGSDKSGKVRWTGTRVDLVFGSHSQLRALAEVYASEDGKEKFAKDFVAAWVKVMNLDRFDLKK","length":750,"molWeight":82199,"crc64":"417D450565CAFBB7","md5":"5A79D20353D9830EE432E78AF901E0F4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI001183E4E1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HV39","uniProtkbId":"A0AAE9HV39_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10577.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Alanine racemase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"5.1.1.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10577.1"}],"value":"alr"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10577.1"}],"value":"FGG12_20990"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanine = D-alanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20249"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57972"}],"ecNumber":"5.1.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Belongs to the alanine racemase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10577.1"}],"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":232,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"Alanine racemase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01005"}]},{"type":"Active site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Proton acceptor; specific for D-alanine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}]},{"type":"Active site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Proton acceptor; specific for L-alanine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}]},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-52"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-52"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10577.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10577.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000014","properties":[{"key":"ProteinId","value":"TSP10577.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144200594.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000013.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HV39","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_08965","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0008784","properties":[{"key":"GoTerm","value":"F:alanine racemase 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:0030632","properties":[{"key":"GoTerm","value":"P:D-alanine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06827","properties":[{"key":"EntryName","value":"PLPDE_III_AR_proteobact"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.10:FF:000002","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.10","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.37.10","properties":[{"key":"EntryName","value":"Lyase, Ornithine Decarboxylase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01201","properties":[{"key":"EntryName","value":"Ala_racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000821","properties":[{"key":"EntryName","value":"Ala_racemase"}]},{"database":"InterPro","id":"IPR009006","properties":[{"key":"EntryName","value":"Ala_racemase/Decarboxylase_C"}]},{"database":"InterPro","id":"IPR011079","properties":[{"key":"EntryName","value":"Ala_racemase_C"}]},{"database":"InterPro","id":"IPR001608","properties":[{"key":"EntryName","value":"Ala_racemase_N"}]},{"database":"InterPro","id":"IPR020622","properties":[{"key":"EntryName","value":"Ala_racemase_pyridoxalP-BS"}]},{"database":"InterPro","id":"IPR029066","properties":[{"key":"EntryName","value":"PLP-binding_barrel"}]},{"database":"NCBIfam","id":"TIGR00492","properties":[{"key":"EntryName","value":"alr"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30511","properties":[{"key":"EntryName","value":"ALANINE RACEMASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30511:SF0","properties":[{"key":"EntryName","value":"ALANINE RACEMASE, CATABOLIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00842","properties":[{"key":"EntryName","value":"Ala_racemase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01168","properties":[{"key":"EntryName","value":"Ala_racemase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00992","properties":[{"key":"EntryName","value":"ALARACEMASE"}]},{"database":"SMART","id":"SM01005","properties":[{"key":"EntryName","value":"Ala_racemase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50621","properties":[{"key":"EntryName","value":"Alanine racemase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51419","properties":[{"key":"EntryName","value":"PLP-binding barrel"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00395","properties":[{"key":"EntryName","value":"ALANINE_RACEMASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPRPIHAVIHQPALANNLDVVRRYAPQSRIWAVVKANAYGHGIRRAFAGMRGTDGFGLLDLNEAVLLRDLGWQGPILLLEGFFQPQDVPLLEQYRLTTAIHCDEQLRMLEVARPRGPLAIQLKLNTGMNRLGFRPEAYRAAWERARGLSCVGSIVHMTHFSDADSARGIAHQIEAFDTATANLPGEASLSNSAAVLWHPQAHRAWVRPGVILYGASPTGIAADIADTGLQPAMSLHSELIAVQDLQPGDTVGYGSMFTADRPMRIGIVACGYADGYPRHAAGWGERPAPVLVDGTRTTLVGRVSMDMVCVDLTPCPKARVGSPVTLWGQGLPIDEVAAASGTVGYELMCALAMRVPCTVATLTTADATA","length":369,"molWeight":39613,"crc64":"68DCCAEB53628B9D","md5":"25F86264B363A84B2717A794F0004AFF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":2,"Modified residue":1},"uniParcId":"UPI001183C2B5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HVS6","uniProtkbId":"A0AAE9HVS6_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10067.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthase small chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthetase glutamine chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10067.1"}],"value":"carA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10067.1"}],"value":"FGG12_24150"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049285"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007800"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10067.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"Carbamoyl-phosphate synthase small subunit N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01097"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"CPSase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]},{"type":"Active site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10067.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10067.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000018","properties":[{"key":"ProteinId","value":"TSP10067.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144201770.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000040.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HVS6","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_10755","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000011","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050472","properties":[{"key":"EntryName","value":"Anth_synth/Amidotransfase"}]},{"database":"InterPro","id":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418:SF7","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418","properties":[{"key":"EntryName","value":"MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLPSFPSAILALADGTVFRGYSIGASGHTIGEVVFNTAITGYQEILTDPSYSRQIVTLTYPHIGNVGVNREDVEATKVHAAGLIIKDLPILASSFRKEHTLAHYLKQEKVVAIAGIDTRKLTRILREKGAQNGCILAGEDNVQKAIDLARSFPGLAGMDLAKVVSVKEPYEWTQNEWKLGEGYGKLDKPQFHVVAYDYGVKFNILRMLAERGCKVTVLPAQASAADALALNPDGIFLSNGPGDPEPCDYAVAATREFIARGIPTFGICLGHQIMALAVGAKTLKMKFGHHGANHPVKDMDDGRVVITSQNHGFAVDAATLPANVRVTHTSLFDGSLQGFTLTDKPAFCFQGHPEASPGPHDVAYLFDRFIKLMKGAKQ","length":378,"molWeight":40824,"crc64":"1C9AFA334EEEF026","md5":"DF1B1501C9DB606C77C8854AA41ABA4C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Active site":3,"Binding site":8},"uniParcId":"UPI000FBA874C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HVY1","uniProtkbId":"A0AAE9HVY1_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11323.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"Ribonuclease 3"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"3.1.26.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"Ribonuclease III"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"RNase III"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"rnc"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11323.1"}],"value":"FGG12_16905"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage to 5'-phosphomonoester.","ecNumber":"3.1.26.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000109"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010183"}],"value":"Belongs to the ribonuclease III family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11323.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"RNase III","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50142"}]},{"type":"Domain","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"DRBM","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50137"}]},{"type":"Region","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}]},{"type":"Active site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}]},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"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_00104"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022664"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_00104"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00104"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11323.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11323.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000010","properties":[{"key":"ProteinId","value":"TSP11323.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144199318.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000054.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HVY1","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_11260","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0003725","properties":[{"key":"GoTerm","value":"F:double-stranded RNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004525","properties":[{"key":"GoTerm","value":"F:ribonuclease III activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006397","properties":[{"key":"GoTerm","value":"P:mRNA processing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010468","properties":[{"key":"GoTerm","value":"P:regulation of gene expression"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006364","properties":[{"key":"GoTerm","value":"P:rRNA processing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd10845","properties":[{"key":"EntryName","value":"DSRM_RNAse_III_family"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00593","properties":[{"key":"EntryName","value":"RIBOc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1520.10:FF:000001","properties":[{"key":"EntryName","value":"Ribonuclease 3"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.160.20:FF:000003","properties":[{"key":"EntryName","value":"Ribonuclease 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.160.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1520.10","properties":[{"key":"EntryName","value":"Ribonuclease III domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00104","properties":[{"key":"EntryName","value":"RNase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR014720","properties":[{"key":"EntryName","value":"dsRBD_dom"}]},{"database":"InterPro","id":"IPR011907","properties":[{"key":"EntryName","value":"RNase_III"}]},{"database":"InterPro","id":"IPR000999","properties":[{"key":"EntryName","value":"RNase_III_dom"}]},{"database":"InterPro","id":"IPR036389","properties":[{"key":"EntryName","value":"RNase_III_sf"}]},{"database":"NCBIfam","id":"TIGR02191","properties":[{"key":"EntryName","value":"RNaseIII"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11207:SF0","properties":[{"key":"EntryName","value":"RIBONUCLEASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11207","properties":[{"key":"EntryName","value":"RIBONUCLEASE III"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00035","properties":[{"key":"EntryName","value":"dsrm"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14622","properties":[{"key":"EntryName","value":"Ribonucleas_3_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00358","properties":[{"key":"EntryName","value":"DSRM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00535","properties":[{"key":"EntryName","value":"RIBOc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54768","properties":[{"key":"EntryName","value":"dsRNA-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69065","properties":[{"key":"EntryName","value":"RNase III domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50137","properties":[{"key":"EntryName","value":"DS_RBD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00517","properties":[{"key":"EntryName","value":"RNASE_3_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50142","properties":[{"key":"EntryName","value":"RNASE_3_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MILDALQQRLGYRFSKPELLQQALTHRSHSAQHNERLEFLGDSVLNCAVADMLYGMFGKLDEGDLSRVRANLVKQQALYEIAQMLQLSDVLRLGEGELKSGGFRRPSILADALEAIVGAVFLDAGFDAARALIRKLYIPILEQVDPRTLGKDAKTLLQEYLQGHKIALPQYNVIATHGAAHSQQFEVECTVPKLEVRVFGTGASRRAAEQAAAKLALDEVQKLVPQLLKRSRAERTGKTRKQPVPPDPQLSLRLKE","length":256,"molWeight":28456,"crc64":"DEBB1A5712D38D6F","md5":"B32135D9B1AFF572DB360CD69BBAFF07"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":2,"Binding site":3},"uniParcId":"UPI000FB1AE28"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HVY4","uniProtkbId":"A0AAE9HVY4_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10728.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"RNA polymerase sigma factor RpoS"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Sigma S"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Sigma-38"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10728.1"}],"value":"rpoS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10728.1"}],"value":"FGG12_21825"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Interacts with the RNA polymerase core enzyme"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Belongs to the sigma-70 factor family. RpoS subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10728.1"}],"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":179,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"RNA polymerase sigma-70","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00715"}]},{"type":"Domain","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"RNA polymerase sigma-70","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00716"}]},{"type":"DNA binding","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Sigma-70 factor domain-1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}]},{"type":"Region","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Sigma-70 factor domain-2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}]},{"type":"Region","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Sigma-70 factor domain-4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}]},{"type":"Motif","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Interaction with polymerase core subunit RpoC","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023082"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"id":"KW-0731","category":"Molecular function","name":"Sigma factor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00959"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10728.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10728.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000014","properties":[{"key":"ProteinId","value":"TSP10728.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144200891.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000055.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HVY4","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_10085","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016987","properties":[{"key":"GoTerm","value":"F:sigma factor activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006352","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription initiation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06171","properties":[{"key":"EntryName","value":"Sigma70_r4"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.601.10:FF:000001","properties":[{"key":"EntryName","value":"RNA polymerase sigma factor SigA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.601.10","properties":[{"key":"EntryName","value":"RNA Polymerase Primary Sigma Factor"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00959","properties":[{"key":"EntryName","value":"Sigma70_RpoS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR014284","properties":[{"key":"EntryName","value":"RNA_pol_sigma-70_dom"}]},{"database":"InterPro","id":"IPR000943","properties":[{"key":"EntryName","value":"RNA_pol_sigma70"}]},{"database":"InterPro","id":"IPR009042","properties":[{"key":"EntryName","value":"RNA_pol_sigma70_r1_2"}]},{"database":"InterPro","id":"IPR007627","properties":[{"key":"EntryName","value":"RNA_pol_sigma70_r2"}]},{"database":"InterPro","id":"IPR007624","properties":[{"key":"EntryName","value":"RNA_pol_sigma70_r3"}]},{"database":"InterPro","id":"IPR007630","properties":[{"key":"EntryName","value":"RNA_pol_sigma70_r4"}]},{"database":"InterPro","id":"IPR013325","properties":[{"key":"EntryName","value":"RNA_pol_sigma_r2"}]},{"database":"InterPro","id":"IPR013324","properties":[{"key":"EntryName","value":"RNA_pol_sigma_r3/r4-like"}]},{"database":"InterPro","id":"IPR012761","properties":[{"key":"EntryName","value":"RNA_pol_sigma_RpoS"}]},{"database":"InterPro","id":"IPR050239","properties":[{"key":"EntryName","value":"Sigma-70_RNA_pol_init_factors"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"NCBIfam","id":"NF004207","properties":[{"key":"EntryName","value":"rpoS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02394","properties":[{"key":"EntryName","value":"rpoS_proteo"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02937","properties":[{"key":"EntryName","value":"sigma70-ECF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30603","properties":[{"key":"EntryName","value":"RNA POLYMERASE SIGMA FACTOR RPO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30603:SF67","properties":[{"key":"EntryName","value":"RNA POLYMERASE SIGMA FACTOR RPOS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00140","properties":[{"key":"EntryName","value":"Sigma70_r1_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04542","properties":[{"key":"EntryName","value":"Sigma70_r2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04539","properties":[{"key":"EntryName","value":"Sigma70_r3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04545","properties":[{"key":"EntryName","value":"Sigma70_r4"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00046","properties":[{"key":"EntryName","value":"SIGMA70FCT"}]},{"database":"SUPFAM","id":"SSF88946","properties":[{"key":"EntryName","value":"Sigma2 domain of RNA polymerase sigma factors"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88659","properties":[{"key":"EntryName","value":"Sigma3 and sigma4 domains of RNA polymerase sigma factors"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00715","properties":[{"key":"EntryName","value":"SIGMA70_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00716","properties":[{"key":"EntryName","value":"SIGMA70_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPRQKTVSSGVVSRTRRPKQPEGKAGVAKSADVVDAEVFGDDPAAEMVPATDEPITPVARAGLRDTDLATDLRVDIAAADEGDDEEAEDEEEEEEAAEAAPEHDDFKTVLHTELAADTVQHYLNRISIKPLLSAPEELHFSTLAKGGDFSARQVMIERNLRLVVSIAKGYLNRGVPLLDLIEEGNLGLMHAIEKFDPTRGFRFSTYATWWIRQSIERAIMNQARTVRLPVHVIRELNQVLRAKRHLEKGGTDGRDASLEDIAHLLGKTPDEVQDVLALNEHTTSLDTPFDLDPGSSLLDFLSDEHNAAPDQEVAHRELENLMKLWLARLSEKHRYVVERRFGLNHIEPATLEELAEEMGLTRERVRQIQQEALVKLKRHFASQGVRKDAVL","length":391,"molWeight":43763,"crc64":"63F2CFBEEC551FCB","md5":"5BB713D4466F546C1AA94F2BFF19DF04"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"DNA binding":1,"Region":5,"Motif":1,"Compositional bias":3},"uniParcId":"UPI000F96C463"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HW03","uniProtkbId":"A0AAE9HW03_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Phosphate acyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"2.3.1.274"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Acyl-ACP phosphotransacylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Acyl-[acyl-carrier-protein]--phosphate acyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Phosphate-acyl-ACP acyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"}],"value":"plsX"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"}],"value":"FGG12_16970"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42292"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:14125"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:59918"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:138651"}],"ecNumber":"2.3.1.274","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Lipid metabolism; phospholipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Homodimer. Probably interacts with PlsY"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Associated with the membrane possibly through PlsY"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Belongs to the PlsX family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11335.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000010","properties":[{"key":"ProteinId","value":"TSP11335.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144199338.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000054.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HW03","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_11325","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0043811","properties":[{"key":"GoTerm","value":"F:phosphate:acyl-[acyl carrier protein] acyltransferase 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:0006644","properties":[{"key":"GoTerm","value":"P:phospholipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.718.10","properties":[{"key":"EntryName","value":"Isopropylmalate Dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00019","properties":[{"key":"EntryName","value":"PlsX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003664","properties":[{"key":"EntryName","value":"FA_synthesis"}]},{"database":"InterPro","id":"IPR012281","properties":[{"key":"EntryName","value":"Phospholipid_synth_PlsX-like"}]},{"database":"NCBIfam","id":"TIGR00182","properties":[{"key":"EntryName","value":"plsX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30100","properties":[{"key":"EntryName","value":"FATTY ACID/PHOSPHOLIPID SYNTHESIS PROTEIN PLSX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30100:SF1","properties":[{"key":"EntryName","value":"PHOSPHATE ACYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02504","properties":[{"key":"EntryName","value":"FA_synthesis"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002465","properties":[{"key":"EntryName","value":"Phsphlp_syn_PlsX"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53659","properties":[{"key":"EntryName","value":"Isocitrate/Isopropylmalate dehydrogenase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIKLAIDCMGGDHGVSVTVPAAISFLSRHDDAEMILVGLPDAIGAQLRKLHAADHPRVTVVAATEVITMDDPVEVALRKKKDSSMRVAATQVKEGRADALISAGNTGALMAVSRYVLKTLEGIERPAIATTIPNEQGWGTTVLDLGANADCEPGHLLQFARMAEAMVSVVDHKDHPTVGLLNIGEEVIKGNEVVKAAGELLRASELNFYGNVEGNDIFKGTTDIVVCDGFVGNVALKSTEGLAKMIGGMIKEEFTRSWFTKLLAAVAMPVLSRLARRLDPARYNGASLLGLRGLVIKSHGSADAHSFEWAIKRGYDAARNGVIERIARVFANKSGATAPATGGPETDAPDPHPDTHAA","length":359,"molWeight":38014,"crc64":"D73BB0BD5B0FE285","md5":"630B050F19977AC4F2FED4B0E6FC2B52"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1},"uniParcId":"UPI001183FBE1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HW65","uniProtkbId":"A0AAE9HW65_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12542.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"1-deoxy-D-xylulose-5-phosphate synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"2.2.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"1-deoxyxylulose-5-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"DXP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"DXPS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"dxs"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12542.1"}],"value":"FGG12_13230"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glyceraldehyde 3-phosphate + pyruvate + H(+) = 1-deoxy-D-xylulose 5-phosphate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12605"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57792"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"2.2.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004980"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011081"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"value":"Belongs to the transketolase family. DXPS subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12542.1"}],"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":319,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"Transketolase-like pyrimidine-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00861"}]},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022977"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"id":"KW-0784","category":"Biological process","name":"Thiamine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00315"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12542.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12542.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000006","properties":[{"key":"ProteinId","value":"TSP12542.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144198119.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000041.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HW65","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_12095","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0008661","properties":[{"key":"GoTerm","value":"F:1-deoxy-D-xylulose-5-phosphate synthase 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:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016114","properties":[{"key":"GoTerm","value":"P:terpenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009228","properties":[{"key":"GoTerm","value":"P:thiamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02007","properties":[{"key":"EntryName","value":"TPP_DXS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07033","properties":[{"key":"EntryName","value":"TPP_PYR_DXS_TK_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.920:FF:000002","properties":[{"key":"EntryName","value":"1-deoxy-D-xylulose-5-phosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000005","properties":[{"key":"EntryName","value":"1-deoxy-D-xylulose-5-phosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000008","properties":[{"key":"EntryName","value":"1-deoxy-D-xylulose-5-phosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.920","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00315","properties":[{"key":"EntryName","value":"DXP_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005477","properties":[{"key":"EntryName","value":"Dxylulose-5-P_synthase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR009014","properties":[{"key":"EntryName","value":"Transketo_C/PFOR_II"}]},{"database":"InterPro","id":"IPR005475","properties":[{"key":"EntryName","value":"Transketolase-like_Pyr-bd"}]},{"database":"InterPro","id":"IPR020826","properties":[{"key":"EntryName","value":"Transketolase_BS"}]},{"database":"InterPro","id":"IPR033248","properties":[{"key":"EntryName","value":"Transketolase_C"}]},{"database":"InterPro","id":"IPR049557","properties":[{"key":"EntryName","value":"Transketolase_CS"}]},{"database":"NCBIfam","id":"TIGR00204","properties":[{"key":"EntryName","value":"dxs"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003933","properties":[{"key":"EntryName","value":"PRK05444.2-2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43322","properties":[{"key":"EntryName","value":"1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43322:SF5","properties":[{"key":"EntryName","value":"1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13292","properties":[{"key":"EntryName","value":"DXP_synthase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02779","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02780","properties":[{"key":"EntryName","value":"Transketolase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00861","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52922","properties":[{"key":"EntryName","value":"TK C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00801","properties":[{"key":"EntryName","value":"TRANSKETOLASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00802","properties":[{"key":"EntryName","value":"TRANSKETOLASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTYTLLNKIDAPADLRKLDRRQLNTLADELRAYVLESVSQTGGHLSSNLGTVELTIALHYVFDTPSDRVVWDVGHQSYPHKILTGRRDRMSTLRQYGGISGFPRRAESEFDTFGTAHSSTSISAALGMALGARTKGEKRVGIAVIGDGAMTAGMAFEAMNNAGVYKDLPLLVVLNDNDMSISPPVGMLNRHLARLLSGQFYAATKKGIERVLSVAPPVLEFAKRLEEHAKGMVVPATLFEEFGFDYIGPIDGHDLDSLVPTLQNIRQRALEGHGPQFLHVVTKKGQGYKLAEADPILYHGPGKFNPAEGIRPSAKPSRKTYTQVFGEWLCDMAAADKRLIGVTPAMREGSGMVEFEKRFPDRYYDVGIAEQHAVTFAGGLACEGLKPVVAIYSTFLQRGYDQLIHDVALQNLPVVFALDRAGLVGADGATHAGAYDIAYLRCIPNMMVMTPADENECRQLLTTAFQQDCPTAVRYPRGAGAGVATEAALTALPVGKGEMRREGHARAGQRVAFLAFGSMLHPALGAAEALDASVANMRFVKPLDVELVKSLAANHDYLVTVEEGSTMGGAGSAVLEALAEAGIDIPVLVLGLPDKFIDHGDPAFLLSQCGLDAAGIERSVRERFAIAEAPVKVATPRVA","length":639,"molWeight":68768,"crc64":"0DEC2273665426E5","md5":"009F1E46011527CC9D0C5BECC93E4A70"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":8},"uniParcId":"UPI0011834FD0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWF8","uniProtkbId":"A0AAE9HWF8_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12385.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Porphobilinogen deaminase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"PBG"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"2.5.1.61"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Hydroxymethylbilane synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"HMBS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Pre-uroporphyrinogen synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12385.1"}],"value":"hemC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12385.1"}],"value":"FGG12_12380"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002869"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13185"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57845"},{"database":"ChEBI","id":"CHEBI:58126"}],"ecNumber":"2.5.1.61","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048169"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"dipyrromethane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60342"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Binds 1 dipyrromethane group covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004735"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"The porphobilinogen subunits are added to the dipyrromethane group"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005638"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Belongs to the HMBS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12385.1"}],"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":22,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01379"}]},{"type":"Domain","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03900"}]},{"type":"Modified residue","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"S-(dipyrrolylmethanemethyl)cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_00260"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12385.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12385.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000006","properties":[{"key":"ProteinId","value":"TSP12385.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144197970.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000015.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWF8","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_12990","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004418","properties":[{"key":"GoTerm","value":"F:hydroxymethylbilane synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd13646","properties":[{"key":"EntryName","value":"PBP2_EcHMBS_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.190.10:FF:000004","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.190.10:FF:000005","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.160.40","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00260","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000860","properties":[{"key":"EntryName","value":"HemC"}]},{"database":"InterPro","id":"IPR022419","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_cofac_BS"}]},{"database":"InterPro","id":"IPR022417","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_N"}]},{"database":"InterPro","id":"IPR022418","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C"}]},{"database":"InterPro","id":"IPR036803","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C_sf"}]},{"database":"NCBIfam","id":"TIGR00212","properties":[{"key":"EntryName","value":"hemC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557:SF0","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01379","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03900","properties":[{"key":"EntryName","value":"Porphobil_deamC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001438","properties":[{"key":"EntryName","value":"4pyrrol_synth_OHMeBilane_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00151","properties":[{"key":"EntryName","value":"PORPHBDMNASE"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54782","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00533","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN_DEAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQAPASPSSSSAAVSRSMPHKLVIASRESRLAMWQAEHVRAALQQYYPSCDVSILGMTTRGDQILDKSLSKVGGKGLFVKELEVAMAEGRADLAVHSLKDVPMELPAGFALTAVMEREDPRDALVSSQFASLDVMPPGTVVGTSSLRREAALRTRYPHLVIKPLRGNLDTRLRKLDAGEFGAIILAAAGLKRLGLGERIRALIEPEASLPAAGQGALGIEIRSDRPELAAWLAPLNHTPTLLAVSAERAVSRRLGGSCQVPLGAHARWRGDALQLDAFVALPDGSRDVRAHAALAVDTLDAAEQLGAAVAGDLLARGAEDVLAALAAAGPT","length":331,"molWeight":34795,"crc64":"1D90EF51B82B18EB","md5":"8B39291E28FD512349C27DBD3A736FB1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Modified residue":1},"uniParcId":"UPI00118219CB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWI8","uniProtkbId":"A0AAE9HWI8_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12325.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Probable cytosol aminopeptidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"3.4.11.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Leucine aminopeptidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"LAP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"3.4.11.10"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Leucyl aminopeptidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"pepA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12325.1"}],"value":"FGG12_12050"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.","ecNumber":"3.4.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000135"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.","ecNumber":"3.4.11.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Binds 2 manganese ions per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Belongs to the peptidase M17 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12325.1"}],"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":27,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Peptidase M17 leucyl aminopeptidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02789"}]},{"type":"Domain","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"Peptidase M17 leucyl aminopeptidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00883"}]},{"type":"Active site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]},{"type":"Active site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022438"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0031","category":"Molecular function","name":"Aminopeptidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12325.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12325.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000006","properties":[{"key":"ProteinId","value":"TSP12325.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144197910.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000034.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWI8","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_13320","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070006","properties":[{"key":"GoTerm","value":"F:metalloaminopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00433","properties":[{"key":"EntryName","value":"Peptidase_M17"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.10:FF:000004","properties":[{"key":"EntryName","value":"Probable cytosol aminopeptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.220.10","properties":[{"key":"EntryName","value":"Leucine Aminopeptidase, subunit E, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.10","properties":[{"key":"EntryName","value":"Zn peptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00181","properties":[{"key":"EntryName","value":"Cytosol_peptidase_M17"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR064115","properties":[{"key":"EntryName","value":"LAP_cs"}]},{"database":"InterPro","id":"IPR011356","properties":[{"key":"EntryName","value":"Leucine_aapep/pepB"}]},{"database":"InterPro","id":"IPR043472","properties":[{"key":"EntryName","value":"Macro_dom-like"}]},{"database":"InterPro","id":"IPR000819","properties":[{"key":"EntryName","value":"Peptidase_M17_C"}]},{"database":"InterPro","id":"IPR023042","properties":[{"key":"EntryName","value":"Peptidase_M17_leu_NH2_pept"}]},{"database":"InterPro","id":"IPR008283","properties":[{"key":"EntryName","value":"Peptidase_M17_N"}]},{"database":"NCBIfam","id":"NF002073","properties":[{"key":"EntryName","value":"PRK00913.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002074","properties":[{"key":"EntryName","value":"PRK00913.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002077","properties":[{"key":"EntryName","value":"PRK00913.2-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11963:SF23","properties":[{"key":"EntryName","value":"CYTOSOL AMINOPEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11963","properties":[{"key":"EntryName","value":"LEUCINE AMINOPEPTIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00883","properties":[{"key":"EntryName","value":"Peptidase_M17"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02789","properties":[{"key":"EntryName","value":"Peptidase_M17_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00481","properties":[{"key":"EntryName","value":"LAMNOPPTDASE"}]},{"database":"SUPFAM","id":"SSF52949","properties":[{"key":"EntryName","value":"Macro domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53187","properties":[{"key":"EntryName","value":"Zn-dependent exopeptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00631","properties":[{"key":"EntryName","value":"CYTOSOL_AP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEFSTKALDWSKAGQNGFLATKTDCLVVGLFEGQSLAGVAKALDVATKGLVARLVKQGDFEGKRGTQLMLHEVAGIGAARVLLVGLGKEAEFSDKAFVEAVRTAVRALSGTRAASALWCLAQQPPAQRDVAWAVITTITLVRDAGYRLLERHPELKRPPKGVGADKPSLRKIVLAVDAADAKQATQAVVRGTAIANGMELTRDLGNLPSNICTPTYLANTARAMAKRHKLKAEILGRKQIEALNMGAFLAVTKGSVEPPQFIVLRYDGAAAKQAPVVLVGKGITFDTGGISLKPGEGMDEMKYDMCGAASVLGTIQAVAEMGLKINVVAVVPSCENMPSGIATKPGDVVTSMSGQTIEILNTDAEGRLILCDALTYVERFKPAAVVDVATLTGACIIALGHVNSGLYARNDLLADQLLDAGRKAMDTAWRMPLDDDYQDQLKSNFADMANIGGRPAGSVTAACFLARYTEKYDWAHLDIAGTAWKSGAAKGATGRPVPLLTQFLMDRAS","length":509,"molWeight":53854,"crc64":"74746C44058B15C9","md5":"6C1D06A73DFD4A1797F0E01204322687"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":7},"uniParcId":"UPI0011831528"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWL5","uniProtkbId":"A0AAE9HWL5_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11413.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"DNA topoisomerase 4 subunit A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"5.6.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"Topoisomerase IV subunit A"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11413.1"}],"value":"parC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11413.1"}],"value":"FGG12_17390"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent breakage, passage and rejoining of double-stranded DNA.","ecNumber":"5.6.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01384"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"Heterotetramer composed of ParC and ParE"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"value":"Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11413.1"}],"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":530,"modifier":"EXACT"}},"description":"Topo IIA-type catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS52040"}]},{"type":"Coiled coil","location":{"start":{"value":454,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Active site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01384"}]},{"type":"Site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}]},{"type":"Site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}]},{"type":"Site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}]},{"type":"Site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"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":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023029"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00936"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11413.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP11413.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000010","properties":[{"key":"ProteinId","value":"TSP11413.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144199478.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000021.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWL5","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_11760","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005694","properties":[{"key":"GoTerm","value":"C:chromosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009330","properties":[{"key":"GoTerm","value":"C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019897","properties":[{"key":"GoTerm","value":"C:extrinsic component of plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003918","properties":[{"key":"GoTerm","value":"F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007059","properties":[{"key":"GoTerm","value":"P:chromosome segregation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00187","properties":[{"key":"EntryName","value":"TOP4c"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.268.10:FF:000001","properties":[{"key":"EntryName","value":"DNA gyrase subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1360.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.120.10.90","properties":[{"key":"EntryName","value":"DNA gyrase/topoisomerase IV, subunit A, C-terminal"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.199.10","properties":[{"key":"EntryName","value":"Topoisomerase II, domain 5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.268.10","properties":[{"key":"EntryName","value":"Topoisomerase, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00936","properties":[{"key":"EntryName","value":"ParC_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006691","properties":[{"key":"EntryName","value":"GyrA/parC_rep"}]},{"database":"InterPro","id":"IPR035516","properties":[{"key":"EntryName","value":"Gyrase/topoIV_suA_C"}]},{"database":"InterPro","id":"IPR013760","properties":[{"key":"EntryName","value":"Topo_IIA-like_dom_sf"}]},{"database":"InterPro","id":"IPR013758","properties":[{"key":"EntryName","value":"Topo_IIA_A/C_ab"}]},{"database":"InterPro","id":"IPR013757","properties":[{"key":"EntryName","value":"Topo_IIA_A_a_sf"}]},{"database":"InterPro","id":"IPR002205","properties":[{"key":"EntryName","value":"Topo_IIA_dom_A"}]},{"database":"InterPro","id":"IPR005742","properties":[{"key":"EntryName","value":"TopoIV_A_Gneg"}]},{"database":"InterPro","id":"IPR050220","properties":[{"key":"EntryName","value":"Type_II_DNA_Topoisomerases"}]},{"database":"NCBIfam","id":"TIGR01062","properties":[{"key":"EntryName","value":"parC_Gneg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004044","properties":[{"key":"EntryName","value":"PRK05561.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43493","properties":[{"key":"EntryName","value":"DNA GYRASE/TOPOISOMERASE SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43493:SF1","properties":[{"key":"EntryName","value":"DNA TOPOISOMERASE 4 SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03989","properties":[{"key":"EntryName","value":"DNA_gyraseA_C"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00521","properties":[{"key":"EntryName","value":"DNA_topoisoIV"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00434","properties":[{"key":"EntryName","value":"TOP4c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101904","properties":[{"key":"EntryName","value":"GyrA/ParC C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56719","properties":[{"key":"EntryName","value":"Type II DNA topoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS52040","properties":[{"key":"EntryName","value":"TOPO_IIA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDQPDISFQSEEPADSLTLARYAERAYLDYAVSVVKGRALPEVADGQKPVQRRILYAMAAMGLRADAKPVKSARVVGEVLGKFHPHGDQSAYDALVRLAQDFSLRYPLIDGQGNFGSRDGDGAAAMRYTEARLTPISRLLLDEIDLGTVDFLPNYDGSEEEPRLLPARLPFVLLNGASGIAVGMATEIPPHNLREVAGATVAMIRNPAISLAELLALMPGPDYPGGGQIISPAADIAQIYEGGRGSLKVRARWKIEEMARGQWQMVVHELPPATSAQKVLEEIEEITNPKIRTGKKALTPEQVQLKTSLLAVLDAVRDESGKDAPVRLVFEPKSKNVDQQEFIQTLLAHTSLESGAPINLVMIGTDGRPRQKGLQEILREWIGFRFETVTRRTRFQLNKVEDRIHILEGRMLVLLKIDEVIRIIRESDEPKPALIEAFQLSDRQAEDILEIRLRQLARLEAIRIEQELAKLRDEQAELDVLLKSETMMRRRIIKEIEQDAKQYSPEDKDPRRTLIQEERRAAAEVRVVDEPVTVIVSGKGWVRTRQGHGHETQQFTFKAGDSLYDTFECRTVDTLLAFGSNGRVYSVAVAGLPGGRGDGVPVTTLIDLAPGSQIAHTFAGGAEQRVLVATAGGNGFVTKVGDMISRQKGGKSFITLDEGDTLLPPAPIADEATHVACFSGNGRLLLVGLDEVKVLSAGGRGVILMELEPKEPLTHAVTVGAPGLLISGTGVRGGKVPPQKLAGKTLLPYVGKRARKGKAVEPRLKEVKIEPVTVDGGS","length":778,"molWeight":84964,"crc64":"6366314930CC306E","md5":"DC479C8E52ACDAF6D73F3D3995163A17"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Coiled coil":1,"Active site":1,"Site":4},"uniParcId":"UPI0011840269"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWQ1","uniProtkbId":"A0AAE9HWQ1_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09753.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Phosphoribosylglycinamide formyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"2.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"5'-phosphoribosylglycinamide transformylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"GAR transformylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"GART"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"purN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09753.1"}],"value":"FGG12_25735"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6R)-10-formyltetrahydrofolate = N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6S)-5,6,7,8-tetrahydrofolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15053"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:143788"},{"database":"ChEBI","id":"CHEBI:147286"},{"database":"ChEBI","id":"CHEBI:195366"}],"ecNumber":"2.1.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005054"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Belongs to the GART family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09753.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Formyl transferase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00551"}]},{"type":"Active site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:143788"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"N(1)-(5-phospho-beta-D-ribosyl)glycinamide","id":"ChEBI:CHEBI:143788"}},{"type":"Binding site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:195366"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"(6R)-10-formyltetrahydrofolate","id":"ChEBI:CHEBI:195366"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:195366"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"(6R)-10-formyltetrahydrofolate","id":"ChEBI:CHEBI:195366"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:195366"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"(6R)-10-formyltetrahydrofolate","id":"ChEBI:CHEBI:195366"}},{"type":"Site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Raises pKa of active site His","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_01930"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09753.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP09753.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000021","properties":[{"key":"ProteinId","value":"TSP09753.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144202385.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000032.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWQ1","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_13755","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0004644","properties":[{"key":"GoTerm","value":"F:phosphoribosylglycinamide formyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd08645","properties":[{"key":"EntryName","value":"FMT_core_GART"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.170:FF:000007","properties":[{"key":"EntryName","value":"Phosphoribosylglycinamide formyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.170","properties":[{"key":"EntryName","value":"Formyl transferase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01930","properties":[{"key":"EntryName","value":"PurN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002376","properties":[{"key":"EntryName","value":"Formyl_transf_N"}]},{"database":"InterPro","id":"IPR036477","properties":[{"key":"EntryName","value":"Formyl_transf_N_sf"}]},{"database":"InterPro","id":"IPR004607","properties":[{"key":"EntryName","value":"GART"}]},{"database":"NCBIfam","id":"TIGR00639","properties":[{"key":"EntryName","value":"PurN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43369","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43369:SF2","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00551","properties":[{"key":"EntryName","value":"Formyl_trans_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53328","properties":[{"key":"EntryName","value":"Formyltransferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKNIVILISGRGSNMEAIVRACAAEQWPGRVAAVLSNRPDASGLAFAAEHGIATGVVDHKQYPDRAGFDAAMRNAIDAHQPDLVVLAGFMRILTPEFVEHYAGRMLNIHPSLLPSFPGLHTHRQALEAGVKFHGATVHFVTPELDHGPIVLQAALDVLPGDTPESLATRLLDCEHVMYPRAVRWFVEDRLQVRDGVVQVQPAEPQWLLALSAPAAGISQ","length":219,"molWeight":23763,"crc64":"4D39BB05C1A85673","md5":"E23C49691D2053E115CD2B48B2FB3233"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":4,"Site":1},"uniParcId":"UPI000FB5CFB3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWW4","uniProtkbId":"A0AAE9HWW4_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12447.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018836"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012153"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"4.1.99.12"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12447.1"}],"value":"ribB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12447.1"}],"value":"FGG12_12705"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"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":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008976"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12447.1"}],"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":208,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"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_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]},{"type":"Site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12447.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP12447.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000006","properties":[{"key":"ProteinId","value":"TSP12447.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144198029.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000015.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWW4","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_12655","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010626","properties":[{"key":"EntryName","value":"ribBA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF34","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIARTEDIIADIRAGRMVILVDEEDRENEGDLVLAADFVTPEAINFMAKYGRGLICLTLTAERCRQLELYPMVSRNGTVHGTNFTVSIEAAEGVTTGISAADRSRTVQAAVARDAKASDLVQPGHIFPLTAQPGGVLIRAGHTEAGCDLGALAGLTPAAVICEIMKDDGTMARLPDLVEFAREHDLKIGTIADLIHYRSRTESIIERAGERTMQTPWGSFQGVIYRDKPTGRAHLALVKGQPRPDTETLVRVHEPLSVLDLLESARTTHSWSLPAALEVLHGAEQGVMVLLNVGDSPEQLFSQFAALDAPQDRPRRKPDLRTYGMGAQILRDLGVGKMRVLGSPQKMPSMTGYDLEVTGCQPMHGEANCD","length":371,"molWeight":40257,"crc64":"85EB1BE18F666E96","md5":"A6B504523EF4FA02443774E8D6D8FDB9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":6,"Site":2},"uniParcId":"UPI0011839F83"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWX4","uniProtkbId":"A0AAE9HWX4_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10100.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Glycerol kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"2.7.1.30"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"ATP:glycerol 3-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Glycerokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"GK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10100.1"}],"value":"glpK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10100.1"}],"value":"FGG12_24345"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycerol + ATP = sn-glycerol 3-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21644"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17754"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57597"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.30","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052101"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Inhibited by fructose 1,6-bisphosphate (FBP)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005190"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009156"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003733"}],"value":"Belongs to the FGGY kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10100.1"}],"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":15,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"Carbohydrate kinase FGGY N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00370"}]},{"type":"Domain","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"Carbohydrate kinase FGGY C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02782"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022798"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0319","category":"Biological process","name":"Glycerol metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_00186"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10100.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10100.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000018","properties":[{"key":"ProteinId","value":"TSP10100.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWX4","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_10950","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0004370","properties":[{"key":"GoTerm","value":"F:glycerol kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019563","properties":[{"key":"GoTerm","value":"P:glycerol catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006072","properties":[{"key":"GoTerm","value":"P:glycerol-3-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07786","properties":[{"key":"EntryName","value":"FGGY_EcGK_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000007","properties":[{"key":"EntryName","value":"Glycerol kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000008","properties":[{"key":"EntryName","value":"Glycerol kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00186","properties":[{"key":"EntryName","value":"Glycerol_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR000577","properties":[{"key":"EntryName","value":"Carb_kinase_FGGY"}]},{"database":"InterPro","id":"IPR018483","properties":[{"key":"EntryName","value":"Carb_kinase_FGGY_CS"}]},{"database":"InterPro","id":"IPR018485","properties":[{"key":"EntryName","value":"FGGY_C"}]},{"database":"InterPro","id":"IPR018484","properties":[{"key":"EntryName","value":"FGGY_N"}]},{"database":"InterPro","id":"IPR005999","properties":[{"key":"EntryName","value":"Glycerol_kin"}]},{"database":"NCBIfam","id":"NF000756","properties":[{"key":"EntryName","value":"glpK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01311","properties":[{"key":"EntryName","value":"glycerol_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10196:SF69","properties":[{"key":"EntryName","value":"GLYCEROL KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10196","properties":[{"key":"EntryName","value":"SUGAR KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02782","properties":[{"key":"EntryName","value":"FGGY_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00370","properties":[{"key":"EntryName","value":"FGGY_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000538","properties":[{"key":"EntryName","value":"GlpK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00933","properties":[{"key":"EntryName","value":"FGGY_KINASES_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00445","properties":[{"key":"EntryName","value":"FGGY_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MERMTPTPSSQQPQYVLALDQGTSSSRAILFDHAGNVVRIAQREFRQYYPHPGHVEHDPYEIWQSQLAVAHEVLGDAGVSGTQIRAIGITNQRETTVLWDRKTGEPVGRALVWQDRRTAPMCEALQAAGHGDTFQQKTGLIIDAYFSGTKLRWMLDHYEGARARAERGELAFGTVDSWLIWQLTDGKRHVTDVSNASRTLLFNIHNFRWDDELLGLLDIPRSLLPDVVPSSGEVARTAARLFGTEIPIAGIAGDQQAATFGQVCFSPGMAKNTYGTGCFILMNAGSQPVTSHNRLLTTIGWQIGNDTQYCLEGGVFMGGATIQWLRDGLKLIQSAPEVEPLARQCEDTGGVVLVPAFAGLGAPHWDPFARGTIVGITRGTGGPHIARAALESIALQSVDVLDAMQKDAGIALAELRVDGGASRSDLLMQMQADLLGTPVVRPRVTETTALGAAYLAGLATGYWADTEEIARQWQVEHRFEPRLSADERGQRLARWHRAVDRARDWARDDAPSA","length":513,"molWeight":56150,"crc64":"230A69DD14C241BE","md5":"0F49E7CF623843FCC74AF12F432FCCF2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":22},"uniParcId":"UPI001182D2DC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HWY2","uniProtkbId":"A0AAE9HWY2_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10412.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013805"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"tRNA-specific 2-thiouridylase MnmA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011949"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"2.8.1.13"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10412.1"}],"value":"mnmA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10412.1"}],"value":"FGG12_23260"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA + AH2 + ATP = 2-thiouridine(34) in tRNA + L-cysteinyl-[protein] + A + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47032"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:11726"},{"database":"Rhea","id":"RHEA-COMP:11727"},{"database":"Rhea","id":"RHEA-COMP:11728"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61963"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:87170"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.8.1.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051542"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006191"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Belongs to the MnmA/TRMU family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10412.1"}],"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":205,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"tRNA-specific 2-thiouridylase MnmA-like central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF20259"}]},{"type":"Domain","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"tRNA-specific 2-thiouridylase MnmA-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF20258"}]},{"type":"Region","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Interaction with target base in tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Region","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Region","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Active site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Disulfide bond","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Alternate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"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_00144"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10412.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10412.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000016","properties":[{"key":"ProteinId","value":"TSP10412.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144201447.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000043.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HWY2","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_14155","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0103016","properties":[{"key":"GoTerm","value":"F:tRNA-uridine 2-sulfurtransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0002143","properties":[{"key":"GoTerm","value":"P:tRNA wobble position uridine thiolation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01998","properties":[{"key":"EntryName","value":"MnmA_TRMU-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.30.280:FF:000001","properties":[{"key":"EntryName","value":"tRNA-specific 2-thiouridylase MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000023","properties":[{"key":"EntryName","value":"tRNA-specific 2-thiouridylase MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000004","properties":[{"key":"EntryName","value":"tRNA-specific 2-thiouridylase MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.280","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like domains"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00144","properties":[{"key":"EntryName","value":"tRNA_thiouridyl_MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004506","properties":[{"key":"EntryName","value":"MnmA-like"}]},{"database":"InterPro","id":"IPR046885","properties":[{"key":"EntryName","value":"MnmA-like_C"}]},{"database":"InterPro","id":"IPR046884","properties":[{"key":"EntryName","value":"MnmA-like_central"}]},{"database":"InterPro","id":"IPR023382","properties":[{"key":"EntryName","value":"MnmA-like_central_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF001138","properties":[{"key":"EntryName","value":"mnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00420","properties":[{"key":"EntryName","value":"trmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11933:SF5","properties":[{"key":"EntryName","value":"MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11933","properties":[{"key":"EntryName","value":"TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03054","properties":[{"key":"EntryName","value":"tRNA_Me_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20258","properties":[{"key":"EntryName","value":"tRNA_Me_trans_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20259","properties":[{"key":"EntryName","value":"tRNA_Me_trans_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGKRVVVGMSGGVDSSVTAWLLKQQGYEVIGLFMKNWEDDDDSEYCSTREDWLDVVSVADLIGVDVEAVNFAAEYKDRVFADFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLGADTIATGHYARVRQADNGRFELLKAFDHTKDQSYFLHRLNQAQLSRTLFPLGEMPKTRVREIAAEIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTKPGPMKTPEGKVVGEHIGLAFYTLGQRKGIGLGGSREGSGDAWYVARKDMASNTLYVVQGHDHPWLLTPVLEAADLSWVAGEPPAAGAEMAAKTRYRQSDAACRVEAANGDVLKLAFAEAQWAVTPGQSAVLYDGDVCLGGGIIQ","length":359,"molWeight":39349,"crc64":"92092F2D86836683","md5":"B5BF7330F8132B4DE840F9C89FBD09C8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":2,"Binding site":3,"Site":2,"Disulfide bond":1},"uniParcId":"UPI000FA87217"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAE9HX09","uniProtkbId":"A0AAE9HX09_9BURK","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cupriavidus campinensis","taxonId":151783,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038983"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"4-hydroxy-tetrahydrodipicolinate reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"HTPA reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038983"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"1.17.1.8"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10397.1"}],"value":"dapB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10397.1"}],"value":"FGG12_23175"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate + NAD(+) + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:35323"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16845"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:67139"}],"ecNumber":"1.17.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049396"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate + NADP(+) + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:35331"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16845"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:67139"}],"ecNumber":"1.17.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037922"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006642"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Belongs to the DapB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10397.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Dihydrodipicolinate reductase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01113"}]},{"type":"Domain","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"Dihydrodipicolinate reductase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF05173"}]},{"type":"Active site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]},{"type":"Active site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]},{"type":"Binding site","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16845"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate","id":"ChEBI:CHEBI:16845"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16845"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate","id":"ChEBI:CHEBI:16845"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022915"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0220","category":"Biological process","name":"Diaminopimelate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3P7QHB0N9FMSH","citationType":"submission","authors":["Abbaszade G.","Szabo A.","Toumi M.","Toth E."],"title":"Whole genome sequence analysis of Cupriavidus campinensis S14E4C strain.","publicationDate":"MAY-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}],"value":"S14E4C","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TSP10397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000318943"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VCIZ01000016","properties":[{"key":"ProteinId","value":"TSP10397.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_144201416.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAJPVH010000082.1"}]},{"database":"AlphaFoldDB","id":"A0AAE9HX09","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ccam:M5D45_14240","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000318943","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:0008839","properties":[{"key":"GoTerm","value":"F:4-hydroxy-tetrahydrodipicolinate reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009085","properties":[{"key":"GoTerm","value":"P:L-lysine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02274","properties":[{"key":"EntryName","value":"DHDPR_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.360.10:FF:000004","properties":[{"key":"EntryName","value":"4-hydroxy-tetrahydrodipicolinate reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000048","properties":[{"key":"EntryName","value":"4-hydroxy-tetrahydrodipicolinate reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00102","properties":[{"key":"EntryName","value":"DapB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022663","properties":[{"key":"EntryName","value":"DapB_C"}]},{"database":"InterPro","id":"IPR000846","properties":[{"key":"EntryName","value":"DapB_N"}]},{"database":"InterPro","id":"IPR022664","properties":[{"key":"EntryName","value":"DapB_N_CS"}]},{"database":"InterPro","id":"IPR023940","properties":[{"key":"EntryName","value":"DHDPR_bac"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00036","properties":[{"key":"EntryName","value":"dapB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20836:SF0","properties":[{"key":"EntryName","value":"4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20836","properties":[{"key":"EntryName","value":"DIHYDRODIPICOLINATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05173","properties":[{"key":"EntryName","value":"DapB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01113","properties":[{"key":"EntryName","value":"DapB_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000161","properties":[{"key":"EntryName","value":"DHPR"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01298","properties":[{"key":"EntryName","value":"DAPB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNIAIAGASGRMGRMLIEHVLNTDGVTLTGALDVPGAAALGQDAGLFLGRTTGVTISSDLDAVLGAADCLIDFTRPEGTLAHVAAARRLGKKMVIGTTGFDAAGKQALADAAKSIAIVFAANMSVGVNATFKLLEVAAKLLSTGYDIEIIEAHHRHKVDAPSGTALAMGEVVAGALGRSLDDCAVYAREGHTGPRDANSIGFATVRGGDIVGDHTVMFAGIGERIEISHKSSSRQSYADGAVRAARFLADKSAGLFDMQDVLGLK","length":265,"molWeight":27188,"crc64":"B359BB40E9508BCD","md5":"75155629FD86AD42EA71D0398F1F0835"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":3},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":5},"uniParcId":"UPI000F91A9A7"}}]}