{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SN58","uniProtkbId":"A0A229SN58_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM60242.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM60242.1"}],"value":"CF165_43230"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM60242.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":543,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":524,"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":526,"modifier":"EXACT"},"end":{"value":526,"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":19,"modifier":"EXACT"},"end":{"value":19,"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":19,"modifier":"EXACT"},"end":{"value":19,"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":20,"modifier":"EXACT"},"end":{"value":25,"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":77,"modifier":"EXACT"},"end":{"value":77,"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":77,"modifier":"EXACT"},"end":{"value":77,"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":151,"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":158,"modifier":"EXACT"},"end":{"value":160,"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":198,"modifier":"EXACT"},"end":{"value":203,"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":198,"modifier":"EXACT"},"end":{"value":203,"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":234,"modifier":"EXACT"},"end":{"value":234,"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":234,"modifier":"EXACT"},"end":{"value":234,"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":252,"modifier":"EXACT"},"end":{"value":252,"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":365,"modifier":"EXACT"},"end":{"value":365,"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":393,"modifier":"EXACT"},"end":{"value":396,"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":416,"modifier":"EXACT"},"end":{"value":416,"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":477,"modifier":"EXACT"},"end":{"value":477,"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":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000064","properties":[{"key":"ProteinId","value":"OXM60242.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093953385.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000064.1"}]},{"database":"AlphaFoldDB","id":"A0A229SN58","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGLQSRATKYVFVTGGVASSLGKGLTASSLGQLLTARGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTDDGAETDLDIGHYERFLDRDLDGKANVTTGQVYSEVIAKERRGEYLGDTVQVIPHITDEIKARITAAAGPDETGQSPDVVITEVGGTVGDIESLPFLEACRQVRHDVGRDQCFFLHVSLVPYLAPSGELKTKPTQHSVAALRNIGIQPDALVCRADREIPEDLKRKIGLMCDVDTEAVIACPDARSIYDIPKVLHREALDAYVVRRLGLPFRDVDWTVWGDLLDRVHNPNEVVRIAVVGKYIDLPDAYLSVTEALRAGGFAHRAKVEIVWVASDDAQTASGAASVLSDVDGVLIPGGFGIRGIEGKVGAIEYARTRGVPLLGLCLGLQCMVIEAARHLAGIEDAGSSEFDENTRHPVISTMADQRDVVAGERDMGGTMRLGAYPAKLKAGSQVAKAYGTTEVSERHRHRYEVNNAYRKQLSDAGLVFSGTSPDDRLVEFVELPAEVHPFFVGTQAHPELKSRPTRPHPLFSAFVKAVVDRKVAERLPVELPEAPVAAR","length":566,"molWeight":61466,"crc64":"D7C9D95B2A395CC2","md5":"75771F727A2DBDC634873F57D4B540AE"},"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":"UPI000B8A9F5D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SPD9","uniProtkbId":"A0A229SPD9_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-10-25","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM60673.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate--fructose 6-phosphate 1-phosphotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"2.7.1.90"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"6-phosphofructokinase, pyrophosphate dependent"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-dependent phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-PFK"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate-dependent 6-phosphofructose-1-kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"pfp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM60673.1"}],"value":"CF165_41125"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57634"}],"ecNumber":"2.7.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Non-allosteric"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM60673.1"}],"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":297,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33019"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"diphosphate","id":"ChEBI:CHEBI:33019"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"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_01976"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000057","properties":[{"key":"ProteinId","value":"OXM60673.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_086845267.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000057.1"}]},{"database":"AlphaFoldDB","id":"A0A229SPD9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802503at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0047334","properties":[{"key":"GoTerm","value":"F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01976","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR012829","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02483","properties":[{"key":"EntryName","value":"PFK_mixed"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF52","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVGVLTGGGDCPGLNAVIRAVVRKGIEVHGWDFVGFRNGWNGPLTGDSRPLGLNDVEDILTRGGTILRSSRTNPYKVEGGVDKIKQVLADQGVDALIAIGGEDTLGVAKRLTDDGVGVVGVPKTIDNDLGATDYTFGFDTAVSIATEAIDRLHTTAESHHRALVVEVMGRHAGWIALHSGLAGGASVILVPERHFNVDQVVSWVERRFEKEFAPIIVVAEGALPEGGEEKLLTGEKDAFGHVRLGGIGTWLADEIAHRTGKESRAVVLGHVQRGGTPTAYDRVLATRFGLNAVDAVADGDFGVMVALKGTDIVRVKLSEATAELKTVPVERYQEAEVFFG","length":341,"molWeight":36258,"crc64":"1A7D905690F7C24E","md5":"AD4A900D901BB29F8800E295510D4D22"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":8,"Site":2},"uniParcId":"UPI000A3A09B8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SSB4","uniProtkbId":"A0A229SSB4_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM61957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM61957.1"}],"value":"CF165_37060"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"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":"OXM61957.1"}],"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":113,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"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":134,"modifier":"EXACT"},"end":{"value":134,"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":182,"modifier":"EXACT"},"end":{"value":183,"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":216,"modifier":"EXACT"},"end":{"value":216,"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":239,"modifier":"EXACT"},"end":{"value":241,"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":318,"modifier":"EXACT"},"end":{"value":318,"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":"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":"UP000215199"}],"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-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000043","properties":[{"key":"ProteinId","value":"OXM61957.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093952251.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000043.1"}]},{"database":"AlphaFoldDB","id":"A0A229SSB4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTALPLVFDAPKRGLPPRHLADLSVAERAAAVAELGEKPFRAKQLSNHYFSRLTVDPAEMTDIPAASRSRLVESLMPTLLTEVRALEADKGATRKTLWRAHDGTLLESVLMRYPDRATLCISSQAGCGMACPFCATGQGGLDRNLSTAEIVDQVRSAAAVMRDGTMPGGPGRLSNIVFMGMGEPLANYKRVVAAVRRITDPAPGGLGIGQRSVTVSTVGLAPAIRKLADEKMQVRLAVSLHTPDDELRDTLVPVNNRWSIDEVLSAARYYADTSGRRVSIEYALIRDINDQPWRAELLAKRLRKHLGQLVHVNVIPLNPTPGSKWDASPKPVEREFVRLVNAGGVACTVRDTRGQEIAAACGQLAAEG","length":368,"molWeight":39783,"crc64":"BF3E1878AC91B7B7","md5":"8EAEC657B59BA7164910E9B37F891F67"},"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":"UPI000B8A6A06"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229STM8","uniProtkbId":"A0A229STM8_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":35,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62172.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenylyl-sulfate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"2.7.1.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"APS kinase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"ATP adenosine-5'-phosphosulfate 3'-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenosine-5'-phosphosulfate kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62172.1"}],"value":"cysC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62172.1"}],"value":"CF165_36100"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002357"}],"value":"APS kinase catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049370"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}],"value":"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005438"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007237"}],"value":"In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62172.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Region","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"G1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"G2","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"G3","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"G4","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"G5","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Active site","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]},{"type":"Binding site","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62172.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"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_00065"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000042","properties":[{"key":"ProteinId","value":"OXM62172.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093952064.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000042.1"}]},{"database":"AlphaFoldDB","id":"A0A229STM8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804504at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00140","properties":[{"key":"RectionId","value":"UER00205"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04166","properties":[{"key":"EntryName","value":"CysN_ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03695","properties":[{"key":"EntryName","value":"CysN_NodQ_II"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04095","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000119","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00065","properties":[{"key":"EntryName","value":"Adenylyl_sulf_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR041757","properties":[{"key":"EntryName","value":"CysN_GTP-bd"}]},{"database":"InterPro","id":"IPR044138","properties":[{"key":"EntryName","value":"CysN_II"}]},{"database":"InterPro","id":"IPR044139","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"}]},{"database":"InterPro","id":"IPR031157","properties":[{"key":"EntryName","value":"G_TR_CS"}]},{"database":"InterPro","id":"IPR054696","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011779","properties":[{"key":"EntryName","value":"SO4_adenylTrfase_lsu"}]},{"database":"InterPro","id":"IPR000795","properties":[{"key":"EntryName","value":"T_Tr_GTP-bd_dom"}]},{"database":"InterPro","id":"IPR050100","properties":[{"key":"EntryName","value":"TRAFAC_GTPase_members"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"InterPro","id":"IPR009001","properties":[{"key":"EntryName","value":"Transl_elong_EF1A/Init_IF2_C"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02034","properties":[{"key":"EntryName","value":"CysN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003013","properties":[{"key":"EntryName","value":"PRK03846.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004035","properties":[{"key":"EntryName","value":"PRK05506.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23115","properties":[{"key":"EntryName","value":"TRANSLATION FACTOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22594","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00009","properties":[{"key":"EntryName","value":"GTP_EFTU"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00315","properties":[{"key":"EntryName","value":"ELONGATNFCT"}]},{"database":"SUPFAM","id":"SSF50465","properties":[{"key":"EntryName","value":"EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00301","properties":[{"key":"EntryName","value":"G_TR_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51722","properties":[{"key":"EntryName","value":"G_TR_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQLLRIATAGSVDDGKSTLIGRLLFDSKAIFTDQLAAVERASRDRGEDYPDLALLTDGLRAEREQGITIDVAHRYFATPRRKFIIADTPGHLQYTRNMVTGASTADLALVLVDARKGVLEQSRRHAFLASLLGIGHLVVCVNKMDLVGWSRERFDEIREDFRRFAMKLDVADLTFVPVSALHGDNVVHRSASMPWYEGTSLLHQLEEVHVASDRNLIDARFPVQYVIRRSDFRGYAGTIAGGVFKPGDEVVALPSGFTSKVRAVWGPGGQPLEEAFTGQAVAVELADDLDLGRGAMLCRPGNRAESAREVDALVCWFSERAALTPGATYSVRHTTTETRGTVDRLEYRLDVTTLHRDETAESLRLNDIGRIRLRTRAPLLFDPYRRNRATGGFLLVDEHTGDTVAAGMITGAVASPVVWHTAAVRREDRPTRGATVWLTGLSASGKSSVAVELERRLVAAGRPAYLLDGDNLRHGLNKGLGFSPEDRAENVRRVAEVARLFADAGVVAIASLISPYEADRARARTVHEGLPFVEVFVDTPLEVCEARDPKGMYAKARAGEITGFTGIDAPYERPSSPDLVLRPGDGDPAAMAAAIQALLDDLG","length":603,"molWeight":65815,"crc64":"1D1671B45ECDCBEB","md5":"62A6463622AA44E4F50EE6B4B3FF0AC9"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":5,"Active site":1,"Binding site":1},"uniParcId":"UPI000B8AFEBD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229STU3","uniProtkbId":"A0A229STU3_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-10-25","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62527.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM62527.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62527.1"}],"value":"CF165_34400"}]}],"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":"OXM62527.1"}],"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":164,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"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":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000040","properties":[{"key":"ProteinId","value":"OXM62527.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A229STU3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGVGGGIAAYKACEVLRGLTESGHDVRVVPTEAALNFVGAATFEALSGHPVHTGVFTEVPEVQHVRVGKEADLVLVVPATANLLAKAAHGLADDLLTNTLLTARCPVAFFPAMHTEMWEHPATRDNVALLRSRGMIVTEPDAGRLTGADTGKGRLANPAEIVDLARLLLARPDALPRDLEGVRVVVSAGGTREPLDPVRYLGNRSSGKQGYALARVAAQRGADVTLVAAHTVALPDPAGAVVRHVSTAEELRQAVHAASEAADVVVMAAAVADFRPANRAEHKIKKSDDQPDPVITLDRNADILAELVRNRRPGQVVVGFAAETGDEQGSVLDHARVKLKRKGADLLVVNAVGDGKAFGTEDNSGWLLGSDGTEIAIPLGAKAELASTLWDAVVRFMKR","length":399,"molWeight":41974,"crc64":"980B54AA4E80ACB5","md5":"B9CFCDE1A4A15865DE5134FA244E5654"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":5},"uniParcId":"UPI000B8B76A5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229STZ8","uniProtkbId":"A0A229STZ8_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":41,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62418.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62418.1"}],"value":"CF165_34335"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043932"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"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_01283"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"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"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"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":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62418.1"}],"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":230,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Proton acceptor; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"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_01283"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000040","properties":[{"key":"ProteinId","value":"OXM62418.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093951744.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000040.1"}]},{"database":"AlphaFoldDB","id":"A0A229STZ8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793111at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00399"}]},{"database":"Proteomes","id":"UP000215199","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: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":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc 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":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"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_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"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":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF006803","properties":[{"key":"EntryName","value":"PRK09311.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","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":"MSETSAAEPEAGWTPCGAGAVFDADAIERAISDIAAGRPVVVVDDEDRENEGDLIFAAEKATPELLAFMVRYTSGYVCVALTEAEADRLDLPPMYHTNQDARGTAYSVTVDAAEGISTGISAADRAHTIRLLADPSSTAKDFRRPGHVVPLRAKEGGVLRRPGHTEASVDLARMAGLAPAGVLCEIVSQKDEGDMARRDELEVFAADHDLAIITIADLIAYRRRTEKQVERVAEARIPLAAGTFRAVGYDSLLDGIEHVAFVYGEIGDGQDILVRVHSECLTGDVFGSLRCDCGPQLEAALEAVAAEGRGVVLYIRGHEGRGIGLLHKLQAYQLQDDGADTVDANLALGVPADARDYGTGAQILCDLGVRTMRLLSNNPAKRIGLEGYGLRVTGRVPLPISPNPENLRYLRTKRDRMGHDLAQLEHYDQVGAGPEHPDGGAL","length":442,"molWeight":47307,"crc64":"4E620E08F854B26F","md5":"F1990EC2019F04C642D4931C80CCC2AD"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI000B8A7B68"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SUW1","uniProtkbId":"A0A229SUW1_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":37,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62434.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM62434.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM62434.1"}],"value":"CF165_34425"}]}],"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":"OXM62434.1"}],"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":138,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":690,"modifier":"EXACT"},"end":{"value":881,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":963,"modifier":"EXACT"},"end":{"value":1108,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":963,"modifier":"EXACT"},"end":{"value":1109,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"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":174,"modifier":"EXACT"},"end":{"value":174,"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":180,"modifier":"EXACT"},"end":{"value":180,"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":181,"modifier":"EXACT"},"end":{"value":181,"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":213,"modifier":"EXACT"},"end":{"value":213,"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":220,"modifier":"EXACT"},"end":{"value":220,"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":246,"modifier":"EXACT"},"end":{"value":246,"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":247,"modifier":"EXACT"},"end":{"value":247,"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":290,"modifier":"EXACT"},"end":{"value":290,"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":290,"modifier":"EXACT"},"end":{"value":290,"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":290,"modifier":"EXACT"},"end":{"value":290,"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":304,"modifier":"EXACT"},"end":{"value":304,"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":304,"modifier":"EXACT"},"end":{"value":304,"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":304,"modifier":"EXACT"},"end":{"value":304,"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":304,"modifier":"EXACT"},"end":{"value":304,"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":304,"modifier":"EXACT"},"end":{"value":304,"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":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":"2"}},{"type":"Binding site","location":{"start":{"value":726,"modifier":"EXACT"},"end":{"value":726,"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":767,"modifier":"EXACT"},"end":{"value":767,"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":772,"modifier":"EXACT"},"end":{"value":772,"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":797,"modifier":"EXACT"},"end":{"value":797,"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":798,"modifier":"EXACT"},"end":{"value":798,"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":799,"modifier":"EXACT"},"end":{"value":799,"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":800,"modifier":"EXACT"},"end":{"value":800,"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":840,"modifier":"EXACT"},"end":{"value":840,"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":840,"modifier":"EXACT"},"end":{"value":840,"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":840,"modifier":"EXACT"},"end":{"value":840,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":854,"modifier":"EXACT"},"end":{"value":854,"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":854,"modifier":"EXACT"},"end":{"value":854,"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"}}],"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":"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":"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":"UP000215199"}],"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"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000040","properties":[{"key":"ProteinId","value":"OXM62434.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093951758.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000040.1"}]},{"database":"AlphaFoldDB","id":"A0A229SUW1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804197at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000215199","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:000014","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":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"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_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":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"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":"1"}]},{"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"}]}],"sequence":{"value":"MPKRTDIQHVLVIGSGPIVIGQAAEFDYSGTQACRVLRSEGLRVSLVNSNPATIMTDPEFADATYIEPVTPDFVEKVIASESERGQPVDALLATLGGQTALNCAVALHERGVLDKYGVELIGADIDAIQRGEDRQKFKDIVRTIGAEVPRSRVCHDMDEVRETVKDLGLPVVIRPSFTMGGLGSGMAHTPEDLERLASTGLAESPVTEVLIEESVLGWKEYELELMRDKHDNVVVVCSIENIDAMGVHTGDSVTVAPTMTLTDREYQVMRDVGIAVLREVGVDTGGCNIQFAINPRDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAIGYTLDEIRNDITGETPAAFEPTLDYVVVKMPRFAFEKFPGADPTLTTTMKSVGEAMSFGRSFPEALGKVMRSIETKATGFWTLPDPEGATVESTLDALRTPHEGRLYEVERALRLGATVEQVHEASGIDPWFIDQIALVGEVGAEVRDAPVLDGDLLRRAKRTGLSDRQIAALRPELAGEDGVRALRHRLGVRPVFKTVDTCAAEFAAKTPYHYSAYESDPDAQSEVAVQSDKPKVLILGSGPNRIGQGIEFDYSCVHAAIALREAGFEAVMVNCNPETVSTDYDTSDRLYFEPLSFEDVLEVVHAEQASGTVAGVIVQLGGQTPLGLAKKLADAGVPVVGTPPEAIHLAEDRGAFGEVLTQAGLPAPRYGTATSFEGAKRIADEIGYPVLVRPSYVLGGRGMEIVYDEESLAGYIRRATEVTPEHPVLVDRFLDDAIEIDVDALFDGEELYLGGVMEHIEEAGIHSGDSSCALPPITLGHTDLQAVRRSTEAIARGVGVRGLLNVQYALKDDVLYVLEANPRASRTVPFVSKATAVPLAKAAALIMTGSTIKDLRESGVLPADGDGGQMPADSPVAVKEAVLPFHRFRTPEGHGVDSLLGPEMKSTGEVMGVDVSFGKAFAKSQSGAYGSLPTSGRVFVSVANRDKRSLVFPVKRLADLGFEILATSGTAEVLRRNGIPCTVVRKHYEGSTEAEPNIVDVILNGDVDMVINTPYGNSGPRIDGYEIRTAAVSRDIPCVTTVQGAAAAVHGIEALIRGDIGVKSLQELQAALKAKS","length":1109,"molWeight":118792,"crc64":"EEDB74131F78C882","md5":"E0FB2BDD1DF68CE2E8DABB8ACAB43512"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":38},"uniParcId":"UPI000B8B080F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SWQ1","uniProtkbId":"A0A229SWQ1_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":35,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM63495.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM63495.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM63495.1"}],"value":"CF165_30275"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056989"},{"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":"OXM63495.1"}],"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":161,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"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":28,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":290,"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":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-127)","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":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000033","properties":[{"key":"ProteinId","value":"OXM63495.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093951003.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000033.1"}]},{"database":"AlphaFoldDB","id":"A0A229SWQ1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9759743at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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":"MSSTQDNPSSAQGVDKKAAAGCPVAHDSVTSHGSESENPAIDSPTPKTGGRPRTNKDWWPNQLDLSVLHAHSSKGNPLGENFSYAKEFAKLDVEALKRDITEVLTTSQDWWPADFGHYGGLMIRLSWHAAGTYRIHDGRGGAGDGNQRFAPLNSWPDNANLDKARRLLWPVKQKYGQKVSWADLLVLAGNVALESMGFKTFGFGFGREDVWEPEEVIWGPEDDWLGDERYVSESEMAPEVGATEMGLIYVNPEGPRGSADFEAAAHFIRETFARMAMNDEETVALIAGGHTFGKTHGAAVADDHVGPEPEGAPLESQGLGWLSTHGTGKGADAITSGLEVTWTDKPTQWSNRFFEILFGFEWELTTSPGGGKQYVAKDAPEIIPDPYDPNKKHKPTMLTTDLSLRFDPVYGPISRRFLENPDEFALAFAKAWYKLLHRDMGPVSRFLGPWVAEPQLWQDPVPAAEGDLVGDADITALKAKVLDSGLSTAELVSTAWASAASFRSTDKRGGANGARIRLEPQRSWEVNQPEQLGKVLEVLEGIQREFNEAGGAQISLADLIVLAGSAAVEKAARDAGVETTVPFHPGRTDASQEQTDTDSFKVLEPRADGFRNYLRSGEKLQPETLLVERAYMLDLTAPEMTVLVGGLRSLGANAGGARHGVLTDRPGLLTNDFFANLLAPGTRWKMSESEENVYEIRDVSTDELKWTATAVDLVFGSNSQLRALSEVYAAEDAREKFVGDFVAAWTKVMELDRFDLA","length":757,"molWeight":82722,"crc64":"16565FBC41ADEBAC","md5":"86037FF4FB1AEE34088875D9E5142C08"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":2,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI000B8AEDF0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229T355","uniProtkbId":"A0A229T355_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":38,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM65523.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM65523.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM65523.1"}],"value":"CF165_23225"}]}],"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":"ARBA","id":"ARBA00005166"},{"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":"ARBA","id":"ARBA00005208"},{"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":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"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":"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:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM65523.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":461,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":467,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":13,"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":24,"modifier":"EXACT"},"end":{"value":24,"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":81,"modifier":"EXACT"},"end":{"value":81,"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":86,"modifier":"EXACT"},"end":{"value":87,"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":110,"modifier":"EXACT"},"end":{"value":112,"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":112,"modifier":"EXACT"},"end":{"value":112,"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":149,"modifier":"EXACT"},"end":{"value":149,"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":164,"modifier":"EXACT"},"end":{"value":164,"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":179,"modifier":"EXACT"},"end":{"value":179,"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":237,"modifier":"EXACT"},"end":{"value":237,"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":237,"modifier":"EXACT"},"end":{"value":237,"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":342,"modifier":"EXACT"},"end":{"value":342,"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":360,"modifier":"EXACT"},"end":{"value":360,"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":375,"modifier":"EXACT"},"end":{"value":375,"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":386,"modifier":"EXACT"},"end":{"value":386,"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":395,"modifier":"EXACT"},"end":{"value":396,"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":432,"modifier":"EXACT"},"end":{"value":432,"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":"UP000215199"}],"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-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000023","properties":[{"key":"ProteinId","value":"OXM65523.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093949922.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000023.1"}]},{"database":"AlphaFoldDB","id":"A0A229T355","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9775031at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:UniProtKB-UniPathway"}]},{"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":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"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":"NF010932","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"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":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"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":"MTGPLSTLILAAGEGTRMRSSTPKVLHPIAGRPLVEHAVRAAAGLNPEHLVVVVGHGREAVGEHLAQVGDTLGRAVGTAVQAEQKGTGHAVSCALATLPPDLTGTVIVSYGDVPLLDTATLGALLDEHTEAKNAVTVLTSVVADPTGYGRIVRDSAGKVTGIVEHKDATPDQAEITEINSGVYAFDAAVLRDGLSRLSTDNAQGELYLTDVLGIANGDGLHVGALVVDDPWLTEGVNDRVQLSALGAELNRRIVQRWQRAGVTIVDPATTWIDAGVSLSRDVVIEPGVQLKGTTSVGEGSTVGPDSTLTNVTIGAGASVVRVHGSDSELGDGVNVGPFTYLRPGTKLGVKAKLGAFVETKAAEIGAGTKVPHLTYVGDATIGEHSNIGCSSVFVNYDGVHKHRTVIGSYVRLGADNTFVAPVHIGDGAYSGAGAVIREDVPPGTLAVSAPPQRNIEGWAIRRRPGTPAAEAAQAALDADPAAGTDRESRA","length":490,"molWeight":50356,"crc64":"2D3624BF17159A7F","md5":"D2168EFE218EDC5568FA63B52067B170"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":4,"Compositional bias":1,"Active site":1,"Binding site":17},"uniParcId":"UPI000B8AE10D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229T864","uniProtkbId":"A0A229T864_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2017-10-25","entryVersion":36,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM66959.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM66959.1"}],"value":"CF165_19545"}]}],"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":"OXM66959.1"}],"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":10,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":66,"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":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"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":304,"modifier":"EXACT"},"end":{"value":304,"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":356,"modifier":"EXACT"},"end":{"value":356,"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":390,"modifier":"EXACT"},"end":{"value":394,"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":419,"modifier":"EXACT"},"end":{"value":419,"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":420,"modifier":"EXACT"},"end":{"value":420,"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":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000016","properties":[{"key":"ProteinId","value":"OXM66959.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093948961.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000016.1"}]},{"database":"AlphaFoldDB","id":"A0A229T864","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9806925at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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":"FunFam","id":"3.40.50.10260:FF:000008","properties":[{"key":"EntryName","value":"Multifunctional fusion protein"},{"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":"MQGIWTTERIREAEGRLFAVTPEGELMRRASFGLSVQLADFLEDHTGGVSGRRVVLLVGSGDNGGDALWAGAFLRRRGVAVTAILLKPEKAHPAGLKALKRAGGRAVSAEDGPQWIARADVVVDGIVGISASGSLRPDAARLVDLVEAPIVAVDLPSGVDPDTGAVDGPAVRATRTVTFGGLKPVHVLAPSWCGEVVLVDIGLRPELGEPQLRRLDIVDVAAAWPVPGPEDDKYSQGVVGIAAGSATYPGAAVLAAGSAVRATSGLVRYAGHAADIVRAQWPEVIATGTVADAGRVQAWVVGPGIGTGSDGRDVLRYVLGQGVPVCADADATTIIAKSPDVLDARDPDTPLVLTPHAGEYERLMGRKPGPDRVTAAREAAKKYNAVVLLKGHCTVIAAPDGRIAVNRPRGAWLATAGSGDVLSGLVGALLAAGSDPWLAAAAAADVHSLAGAIAAQNAPTSASGLVHAIPEAIRAIRSLTS","length":481,"molWeight":49160,"crc64":"EF30822A55AC693D","md5":"2E9E7A87F2164C40521A7B88AFC60B8D"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI000B8B71FA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229TCA1","uniProtkbId":"A0A229TCA1_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-10-25","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM68788.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"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":"OXM68788.1"}],"value":"CF165_11955"}]}],"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":"OXM68788.1"}],"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":41,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"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":133,"modifier":"EXACT"},"end":{"value":139,"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":175,"modifier":"EXACT"},"end":{"value":176,"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":202,"modifier":"EXACT"},"end":{"value":202,"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":210,"modifier":"EXACT"},"end":{"value":210,"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":400,"modifier":"EXACT"},"end":{"value":400,"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":424,"modifier":"EXACT"},"end":{"value":427,"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":477,"modifier":"EXACT"},"end":{"value":477,"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":481,"modifier":"EXACT"},"end":{"value":481,"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":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM68788.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000009","properties":[{"key":"ProteinId","value":"OXM68788.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093947544.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000009.1"}]},{"database":"AlphaFoldDB","id":"A0A229TCA1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9800958at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAVPAPPRPARIVPVPLATLLARADARLIAGSPDAAELTVTGTTLRAQHVLPGDLFAALPGARAHGADFSDQAVAAGAVAVLTDADGAERPALRDAGVPILVHADPRAALGEIAAWIYGEPSLRLAVLGVTGTSGKTTTSYLVDAGLQAAGLTTGLIGTVETRIAGERLVSGFTTPEAPDLQALLAVMLERGVTHVPMEVSSHALALGRVNGTRFAVGAFTNLSQDHLDFHKDMQEYFAAKSLLFDGRSTTEVVVVDSAWGQALLTPQTITVTTDPGTDAAWKATDLEATPQGEQTFTLDGPDGVSARARIPLPGEFNVANAVLAAAILSTAGVGIEHIVAGLAQVQVPGRMERVYVGQEFTAVVDYAHKPAAVAQGLDALRARADGRIITVLGCGGDRDTAKRPMMGEAAARRSEVLIVTDDNPRSEDPAAIRAAMLAGARAAGPAEIIEIADRREAIAHAVSLAEPGDIVFLAGKGHESGQEAGGVVHPFSDRDELAAAIRNKLEVSV","length":511,"molWeight":52828,"crc64":"AA98E05ABA0C7C38","md5":"110B04AFE27DD3B1C5606E3675327EFD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":9,"Modified residue":1},"uniParcId":"UPI000B8A64BE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229TG30","uniProtkbId":"A0A229TG30_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM69901.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM69901.1"}],"value":"CF165_06195"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"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"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM69901.1"}],"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":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000006","properties":[{"key":"ProteinId","value":"OXM69901.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093946445.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000006.1"}]},{"database":"AlphaFoldDB","id":"A0A229TG30","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9810320at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00245","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"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"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSEPVIGVLAMQGAVREHVAMLAEAGARAKPVRRAAELSEVDGLVLPGGESTAMSRLLESFELLEPLRARIAEGLPAFGSCAGMILLARQTLDGRPDQQQLGGLDVVVRRNAFGRQVDSFEADLDFAGIETPPVHAVFIRAPWVEKAGDGVDVLATVSGVPGVDEETARIVAVRQGAVLATAFHPELTPDVRVHRLFVDLVRKAA","length":206,"molWeight":21891,"crc64":"1ECD3A79EABD240D","md5":"E1B7B10AE46DF1547C8F241BC08F840D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI000B8ACB82"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229TI58","uniProtkbId":"A0A229TI58_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-10-25","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70936.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00069359"}],"value":"Broad-specificity linear acyl-CoA dehydrogenase FadE5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012033"}],"value":"1.3.8.7"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"1.3.8.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077090"}],"value":"Long-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077336"}],"value":"Medium-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075470"}],"value":"Short-chain-acyl-CoA dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70936.1"}],"value":"CF165_03390"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054301"}],"value":"Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17721"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83721"},{"database":"ChEBI","id":"CHEBI:83727"}],"ecNumber":"1.3.8.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049247"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14477"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83723"},{"database":"ChEBI","id":"CHEBI:83726"}],"ecNumber":"1.3.8.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047882"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050315"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050695"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"decanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48176"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61406"},{"database":"ChEBI","id":"CHEBI:61430"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050703"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57330"},{"database":"ChEBI","id":"CHEBI:57375"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050336"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048375"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47240"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57394"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:71412"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050877"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43448"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61526"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052387"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004872"}],"value":"Lipid metabolism; fatty acid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70936.1"}],"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":162,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Domain","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":607,"modifier":"EXACT"}},"description":"Acetyl-CoA dehydrogenase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12806"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000004","properties":[{"key":"ProteinId","value":"OXM70936.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093945927.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000004.1"}]},{"database":"AlphaFoldDB","id":"A0A229TI58","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9807883at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004466","properties":[{"key":"GoTerm","value":"F:long-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070991","properties":[{"key":"GoTerm","value":"F:medium-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0016937","properties":[{"key":"GoTerm","value":"F:short-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"2.40.110.20:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase AidB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000016","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase FadE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR025878","properties":[{"key":"EntryName","value":"Acyl-CoA_dh-like_C_dom"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"InterPro","id":"IPR052166","properties":[{"key":"EntryName","value":"Diverse_Acyl-CoA_DH"}]},{"database":"PANTHER","id":"PTHR42803","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42803:SF1","properties":[{"key":"EntryName","value":"BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12806","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGHYKSNVRDLEFNLFEVLGVQERLGKGVLAESDEETARGVLSELNKLATGPLAESFADADRNPPVYDPKTFSVTIPESFKKSYQQLVDGEWWRLGLTNDLGGFGLPPTVQWAASELILGANAPLFMYMAGPNFAMIVDKNGTEEQKHWARIMIDKGWGATMVLTEPDAGSDVGAGRTKATQQEDGSWHIDGVKRFITSGENDMVENIMHLVLARPEGPGIETKPGTKGLSLFLVPKFHFDSETGELGERNGAFVTNIEHKMGIKASTTCELTFGQHGTPAKGWLLGEVHDGIAQMFQVIEYARMMVGTKAIATLSTGYLNALEYAKERVQGADLPNMLNKAAPRVTITHHPDVRRSLMLQKAYSEGLRAVYLYTASFQDQLWTGEGDLKLAHGVNDLLLPIVKGVGSERATEQLVQSLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQSLDFFFRKIVRDKGQSLAFIAGEITKFIESEAGNGRLKNERGLLKQALEDTQGMLGSLIGYLTASQEDAQSINKVGQHTVRLLMSVGDLLIGWQLLKHAEVALTKLDAGASTKDVPFYEGKVAVASFFAKQVLPELTARRAIVEAADNALMEIDEAAF","length":611,"molWeight":66922,"crc64":"6B397F85AC122DC5","md5":"8EE5469318C6EBF14843885B40B939F7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":9,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI000B8B5858"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229TIF5","uniProtkbId":"A0A229TIF5_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":38,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70893.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Phosphoenolpyruvate carboxykinase [GTP]"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"PEP carboxykinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"PEPCK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"4.1.1.32"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"GTP-dependent phosphoenolpyruvate carboxykinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"GTP-PEPCK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"pckG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70893.1"}],"value":"CF165_03135"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxaloacetate + GTP = phosphoenolpyruvate + GDP + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10388"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:58702"}],"ecNumber":"4.1.1.32","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10113"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Binds 1 Mn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004742"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005796"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Belongs to the phosphoenolpyruvate carboxykinase [GTP] family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70893.1"}],"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":243,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate carboxykinase GTP-utilising N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF17297"}]},{"type":"Domain","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate carboxykinase C-terminal P-loop","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00821"}]},{"type":"Region","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10113"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70893.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70893.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM70893.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000004","properties":[{"key":"ProteinId","value":"OXM70893.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093945884.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000004.1"}]},{"database":"AlphaFoldDB","id":"A0A229TIF5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9758871at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00138","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004613","properties":[{"key":"GoTerm","value":"F:phosphoenolpyruvate carboxykinase (GTP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071333","properties":[{"key":"GoTerm","value":"P:cellular response to glucose stimulus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006107","properties":[{"key":"GoTerm","value":"P:oxaloacetate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019543","properties":[{"key":"GoTerm","value":"P:propionate catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033993","properties":[{"key":"GoTerm","value":"P:response to lipid"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042594","properties":[{"key":"GoTerm","value":"P:response to starvation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00819","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.449.10:FF:000005","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate carboxykinase [GTP]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.228.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.449.10","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate Carboxykinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.8.10","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate Carboxykinase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00452","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018091","properties":[{"key":"EntryName","value":"PEP_carboxykin_GTP_CS"}]},{"database":"InterPro","id":"IPR013035","properties":[{"key":"EntryName","value":"PEP_carboxykinase_C"}]},{"database":"InterPro","id":"IPR008209","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP"}]},{"database":"InterPro","id":"IPR035077","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP_C"}]},{"database":"InterPro","id":"IPR035078","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP_N"}]},{"database":"InterPro","id":"IPR008210","properties":[{"key":"EntryName","value":"PEP_carboxykinase_N"}]},{"database":"NCBIfam","id":"NF003253","properties":[{"key":"EntryName","value":"PRK04210.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11561","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE CARBOXYKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11561:SF0","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE CARBOXYKINASE [GTP]-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00821","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17297","properties":[{"key":"EntryName","value":"PEPCK_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001348","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF68923","properties":[{"key":"EntryName","value":"PEP carboxykinase N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53795","properties":[{"key":"EntryName","value":"PEP carboxykinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00505","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAVAIPGLDTAPTTHSGVLSFVREVAELTTPDRVVWVDGSDEEAARINQELVEAGTFVQLKSKPNSFWATSDPNDVARVEDRTFICSERPEDAGPTNNWMDPAEMKATMTELFRGSMRGRTMYVIPFCMGPLGDENPKLGIEITDFAYVVASMRVMTRAGKAALEKFVAPDGSEREFVPALHSVGKPLEPGEKDVSWPCNETKYISHFPEERAIWSYGSGYGGNSLLGKKCYSLRIASVMARDEGWLAEHMLILKLISPEDKVHYVAAAFPSACGKTNLAMLQPTIPGWRAETLGDDIAWMRFGEDGRLYAVNPEFGFFGVAPGTDWHTNPNAMRTIEKGNTVFTNVALTDDGDIWWEGMENKPAHATSWKHQDWTPDSDEKAAHPNSRYCTPMSQCPILAPEWDDPKGVPISAILFGGRRKTTVPLVNEARDWQHGVFMGATMSSETTAAAAGAVGNVRRDPMAMLPFLGYHAGDYFKHWLNLGKNADANKLPKIFYVNWFRRGDDGRFLWPGFGENSRILKWVVERVEGRGNAVETPVGFVPRAEDLDTEGLTEPIEDIQAALDVKPEEWREELPLIEEWFDKIGDRVPTSLRDELDALAQRLA","length":607,"molWeight":67547,"crc64":"BA37626238F474A6","md5":"9787557D7A5DB39A271C72CCB1BA55E5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":11},"uniParcId":"UPI000B8B8B84"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SJW4","uniProtkbId":"A0A229SJW4_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-10-25","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Anhydro-N-acetylmuramic acid kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"2.7.1.170"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"AnhMurNAc kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"anmK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59212.1"}],"value":"CF165_48835"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = N-acetyl-D-muramate 6-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24952"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58690"},{"database":"ChEBI","id":"CHEBI:58722"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.170","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Cell wall biogenesis; peptidoglycan recycling"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Belongs to the anhydro-N-acetylmuramic acid kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59212.1"}],"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":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59212.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000090","properties":[{"key":"ProteinId","value":"OXM59212.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A229SJW4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9763949at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00343","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00544","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0016773","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, alcohol group as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097175","properties":[{"key":"GoTerm","value":"P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006040","properties":[{"key":"GoTerm","value":"P:amino sugar metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009254","properties":[{"key":"GoTerm","value":"P:peptidoglycan turnover"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01270","properties":[{"key":"EntryName","value":"AnhMurNAc_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005338","properties":[{"key":"EntryName","value":"Anhydro_N_Ac-Mur_kinase"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"NCBIfam","id":"NF007146","properties":[{"key":"EntryName","value":"PRK09585.2-6"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30605","properties":[{"key":"EntryName","value":"ANHYDRO-N-ACETYLMURAMIC ACID KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30605:SF0","properties":[{"key":"EntryName","value":"ANHYDRO-N-ACETYLMURAMIC ACID KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03702","properties":[{"key":"EntryName","value":"AnmK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGPDWAKTSPRGLRHTGSSTKPLRMGTHGFRVIGLISGTSVDGIDVAAGDLHAEDGTVVLTPLGELDVPYPEPLREALLAALPPNPCTAGELTRLDTGVGQAFADAARRGAEELAGGRGDLVASLGQTVFHWVEDGQVLGTLQLGQPAWIAERTGLPVCADLRARDVAAGGHGAPLASTLDQLWLRGLAEDTGRPVAALNLGGIANITVVAAGEPATAYDTGPANALLDLAAHRVTGRRSDVDGRLALAGSVRPDLLDRLLADPYFAAAPPKSTGKEHFNAPYLDTATGGLDPIDPADLLATLTELTAVTVADQCRRHGVSTVIASGGGVANPAVMTALARNLGGSTVLKTSDELGLPGAGKEAYLTALLGWLTWCGAPGTVPSATGARGPRLLGALVPGAGPLILPAPLGGTVTRLRVAEKAGQTVGEIHARC","length":434,"molWeight":44178,"crc64":"A8B9D4175E414B1A","md5":"949B453FE3E384B51B08B86788F48D4A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Binding site":1},"uniParcId":"UPI000B8B5F29"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SJX5","uniProtkbId":"A0A229SJX5_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59267.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018543"}],"value":"4-aminobutyrate aminotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012912"}],"value":"2.6.1.19"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012876"}],"value":"2.6.1.22"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030857"}],"value":"(S)-3-amino-2-methylpropionate transaminase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031787"}],"value":"GABA aminotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030204"}],"value":"Gamma-amino-N-butyrate transaminase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050054"}],"value":"Glutamate:succinic semialdehyde transaminase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029760"}],"value":"L-AIBAT"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59267.1"}],"value":"gabT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59267.1"}],"value":"CF165_48460"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13993"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57700"},{"database":"ChEBI","id":"CHEBI:58655"}],"ecNumber":"2.6.1.22","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001750"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23352"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57706"},{"database":"ChEBI","id":"CHEBI:59888"}],"ecNumber":"2.6.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048021"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005176"}],"value":"Amino-acid degradation; 4-aminobutanoate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008954"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003560"}],"value":"Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59267.1"}],"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":"ARBA00022576"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023194"}],"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003560"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000088","properties":[{"key":"ProteinId","value":"OXM59267.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954363.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000088.1"}]},{"database":"AlphaFoldDB","id":"A0A229SJX5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801052at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0047298","properties":[{"key":"GoTerm","value":"F:(S)-3-amino-2-methylpropionate:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0034386","properties":[{"key":"GoTerm","value":"F:4-aminobutyrate:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00610","properties":[{"key":"EntryName","value":"OAT_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000013","properties":[{"key":"EntryName","value":"4-aminobutyrate aminotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004632","properties":[{"key":"EntryName","value":"4NH2But_aminotransferase_bac"}]},{"database":"InterPro","id":"IPR005814","properties":[{"key":"EntryName","value":"Aminotrans_3"}]},{"database":"InterPro","id":"IPR049704","properties":[{"key":"EntryName","value":"Aminotrans_3_PPA_site"}]},{"database":"InterPro","id":"IPR050103","properties":[{"key":"EntryName","value":"Class-III_PLP-dep_AT"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR00700","properties":[{"key":"EntryName","value":"GABAtrnsam"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004714","properties":[{"key":"EntryName","value":"PRK06058.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11986","properties":[{"key":"EntryName","value":"AMINOTRANSFERASE CLASS III"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11986:SF58","properties":[{"key":"EntryName","value":"LEUCINE_METHIONINE RACEMASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00202","properties":[{"key":"EntryName","value":"Aminotran_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000521","properties":[{"key":"EntryName","value":"Transaminase_4ab_Lys_Orn"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00600","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTASTTAEPQAPAPRQRTLRTEIPGPLSRQLQERRANAVAAGVSSVLPVYVTSASGGLLTDADGNVLIDFGSGIAVTNVGHSAPAVVDRVRKQACWFTHTCFMVTPYEGYVEVCEALAELTPGDHAKKSVLFNSGAEAVENAVKIARTATGRQAVVVFDHAYHGRTNLTMGMTAKSVPYKHGFGPFAPEIYRVPGSYPFRDGLSGPEAAALAIDRIEKQIGGDQVAAVVLEPIQGEGGFIEPARGFLPAIAAWCRENGVVYVADEVQTGFCRTGSWFASTDEDVVPDLIATAKGIAGGLPLSAVTGRASLLDAVPPGGLGGTYGGNPIACAAALGSIETMKNEDLAASAKRIEGIVLPRLRALASETGVIGDVRGRGAMLAAEFVKPGSVEPDPDLTKRVAAACHRAGVIVLTCGTYGNVVRLLPPLSLADDLLDEGLSVLEHAVRTEARA","length":451,"molWeight":46961,"crc64":"9EE2EBC7C62B8754","md5":"F43D76417DAE541469A3E542AD53D183"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"uniParcId":"UPI000B8A7E5B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SJY9","uniProtkbId":"A0A229SJY9_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59242.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NADH-quinone oxidoreductase subunit H"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NADH dehydrogenase I subunit H"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH-1 subunit H"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"nuoH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59242.1"}],"value":"CF165_48695"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Belongs to the complex I subunit 1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59242.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Region","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000089","properties":[{"key":"ProteinId","value":"OXM59242.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954405.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000089.1"}]},{"database":"AlphaFoldDB","id":"A0A229SJY9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803734at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0003954","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016655","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"HAMAP","id":"MF_01350","properties":[{"key":"EntryName","value":"NDH1_NuoH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001694","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_su1/FPO"}]},{"database":"InterPro","id":"IPR018086","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_su1_CS"}]},{"database":"NCBIfam","id":"NF004741","properties":[{"key":"EntryName","value":"nuoH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004743","properties":[{"key":"EntryName","value":"nuoH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11432","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11432:SF3","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00146","properties":[{"key":"EntryName","value":"NADHdh"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00668","properties":[{"key":"EntryName","value":"COMPLEX1_ND1_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTPLLTEAAVGSVPDAATRAALLADDPLWLILLKCVVILLIGPILTIFLIVWERKAVGRMQNRPGPNRVGPGGYLQSLADAIKLPFKEQIIPDTADRKVYFLAPVVCVVPSLIALSAIPFGPVVSIFGERTVLQLLDLPVSALVILACSSIGVYGIVLAGWSSGSPYPLLGGMRSAAQVISYEIAMGLSIVAVILQAGSLNLADIVGAQHKAWFLYLVPSFVIYLISMVGETNRAPFDLPEAESELVGGFHTEYSSMKFAMFFLAEYVNMVIVSAFATTLFLGGWMAPWPLSLIGNNVLNTGWWPVLWFFAKMFVLLFGFIWLRGTLPRLRYDQFMRLGWKVLVPLNLVWIVMVTFAKVITWNTTTIIIAAVAIFIVLALFFYVRAAGREEESESVPVTGGGFPVPPLDLKVPQTTPRQKALAKAEAKAARRKPAAVGTAKEGAQDGVS","length":449,"molWeight":48751,"crc64":"857728084813F2DB","md5":"406D80DD7CEC29178E2811509F033816"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":9,"Region":1},"uniParcId":"UPI000B8A996E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SK28","uniProtkbId":"A0A229SK28_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":31,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59248.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NADH-quinone oxidoreductase subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NADH dehydrogenase I subunit B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH-1 subunit B"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"nuoB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59248.1"}],"value":"CF165_48725"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009173"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"value":"Belongs to the complex I 20 kDa subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59248.1"}],"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":37,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"NADH:ubiquinone oxidoreductase-like 20kDa subunit","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01058"}]},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000089","properties":[{"key":"ProteinId","value":"OXM59248.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954411.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000089.1"}]},{"database":"AlphaFoldDB","id":"A0A229SK28","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9786737at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0045271","properties":[{"key":"GoTerm","value":"C:respiratory chain complex I"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050136","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (quinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.40.50.12280:FF:000004","properties":[{"key":"EntryName","value":"NADH-quinone oxidoreductase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12280","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01356","properties":[{"key":"EntryName","value":"NDH1_NuoB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006137","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase-like_20kDa"}]},{"database":"InterPro","id":"IPR006138","properties":[{"key":"EntryName","value":"NADH_UQ_OxRdtase_20Kd_su"}]},{"database":"NCBIfam","id":"NF005012","properties":[{"key":"EntryName","value":"nuoB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01957","properties":[{"key":"EntryName","value":"nuoB_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11995","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11995:SF14","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01058","properties":[{"key":"EntryName","value":"Oxidored_q6"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56770","properties":[{"key":"EntryName","value":"HydA/Nqo6-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01150","properties":[{"key":"EntryName","value":"COMPLEX1_20K"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGLEEKLPNGVLLASLEGLVNWARKNSLWPATFGLACCAIEMMTVGGSRYDIARFGMERFSATPRQADLMIVAGRVTQKMAPVLRQIYDQMAEPRWVLAMGVCASSGGMFNNYAVVQGVDHIVPVDMYLPGCPPRPEMLLDAILKLHAKIQDEPINARRAAIRAASGARTELVASSIKYAKK","length":182,"molWeight":19893,"crc64":"C9549BF58490BCAF","md5":"6F4E3BC2963D13CFBFD96F7544FD26A8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI000B8AD0F2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SK48","uniProtkbId":"A0A229SK48_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2017-10-25","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59213.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Signal recognition particle receptor FtsY"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"SRP receptor"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"3.6.5.4"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"ftsY"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59213.1"}],"value":"CF165_48840"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Belongs to the GTP-binding SRP family. FtsY subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59213.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":402,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"SRP54-type proteins GTP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00300"}]},{"type":"Region","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023170"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0675","category":"Molecular function","name":"Receptor"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000090","properties":[{"key":"ProteinId","value":"OXM59213.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954432.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000090.1"}]},{"database":"AlphaFoldDB","id":"A0A229SK48","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804720at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005047","properties":[{"key":"GoTerm","value":"F:signal recognition particle binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006614","properties":[{"key":"GoTerm","value":"P:SRP-dependent cotranslational protein targeting to membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.20.120.140:FF:000002","properties":[{"key":"EntryName","value":"Signal recognition particle receptor FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000053","properties":[{"key":"EntryName","value":"Signal recognition particle receptor FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.140","properties":[{"key":"EntryName","value":"Signal recognition particle SRP54, nucleotide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00920","properties":[{"key":"EntryName","value":"FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR013822","properties":[{"key":"EntryName","value":"Signal_recog_particl_SRP54_hlx"}]},{"database":"InterPro","id":"IPR004390","properties":[{"key":"EntryName","value":"SR_rcpt_FtsY"}]},{"database":"InterPro","id":"IPR036225","properties":[{"key":"EntryName","value":"SRP/SRP_N"}]},{"database":"InterPro","id":"IPR000897","properties":[{"key":"EntryName","value":"SRP54_GTPase_dom"}]},{"database":"InterPro","id":"IPR042101","properties":[{"key":"EntryName","value":"SRP54_N_sf"}]},{"database":"NCBIfam","id":"TIGR00064","properties":[{"key":"EntryName","value":"ftsY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43134","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43134:SF1","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00448","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02881","properties":[{"key":"EntryName","value":"SRP54_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00962","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00963","properties":[{"key":"EntryName","value":"SRP54_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47364","properties":[{"key":"EntryName","value":"Domain of the SRP/SRP receptor G-proteins"},{"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":"PS00300","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSTWFLFVVVAVVVLVALLVTGLLIARRRRISLDAQREVEEKKPKGGSYAASGGIALAPGGTAEAEAPEHPVEDRPEVDGQPAVGDDAAVPRDSAQRTLRDVKLPEAPEEPAPATEEIDPATGRLERLRGRLSKSRSVLGTSLLGLLGAGDLDEDSWQDVEDTLLMADLGAATTNQIVERLRDELSRRAVRSSAEAREVLHEVLTAQLSTDSERAVRALPHIVDGKKQPAVVLVAGVNGTGKTTTTGKLARVLVAQDKSVVLGAADTFRAAAADQLQTWAERVGAEVVRGKEGADPAAVAFDAVKRGIDTGVDAVLVDTAGRLHTKTGLMDELGKVKRVVEKQAKVDEVLLVLDATTGQNGLMQARVFAEVIDVTGIVLTKLDGTAKGGIVFQVQKELGVPVKLVGLGEGPDDLAPFEPGAFVDALLG","length":429,"molWeight":45124,"crc64":"F38015B53B0C2B13","md5":"06EFC12DDB744366C4CB4BD6C92820E9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":3,"Binding site":3},"uniParcId":"UPI000B8B31DD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SK81","uniProtkbId":"A0A229SK81_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59236.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NADH-quinone oxidoreductase subunit N"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NADH dehydrogenase I subunit N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NDH-1 subunit N"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"nuoN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59236.1"}],"value":"CF165_48665"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000320"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000320"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"Belongs to the complex I subunit 2 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59236.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Domain","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"NADH:quinone oxidoreductase/Mrp antiporter transmembrane","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00361"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000089","properties":[{"key":"ProteinId","value":"OXM59236.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954401.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000089.1"}]},{"database":"AlphaFoldDB","id":"A0A229SK81","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9811718at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0050136","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (quinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042773","properties":[{"key":"GoTerm","value":"P:ATP synthesis coupled electron transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"HAMAP","id":"MF_00445","properties":[{"key":"EntryName","value":"NDH1_NuoN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010096","properties":[{"key":"EntryName","value":"NADH-Q_OxRdtase_suN/2"}]},{"database":"InterPro","id":"IPR001750","properties":[{"key":"EntryName","value":"ND/Mrp_TM"}]},{"database":"NCBIfam","id":"TIGR01770","properties":[{"key":"EntryName","value":"NDH_I_N"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004441","properties":[{"key":"EntryName","value":"nuoN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22773","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00361","properties":[{"key":"EntryName","value":"Proton_antipo_M"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLDILLTQAPTPIATPSVDYPAVLPVLIVFGAACVSVLVEAFAAKRSRFGIQVGLSLLAIIGAGVALIVYATGNAPAAGVTTFSKSISIDRPALFLWGTLLALAFGAVLLISDRVVEPGGALVAQAGIRPGTVQDRAQTATVMQTEVFPLTLFALGGMMAFCAANDLLTMFIALEVLSLPLYLMCGLARRRRLLSQEAAVKYFLLGAFSSAFFLYGLALLYGYANSVKLGDIANAAAGSDRSDTLLFAGLGLLVVGLLFKGSVGPFHTWTPDVYQGAPTPVTAFMAACTKVAAFGGILRVLSVAFSSTSWEWRGVLWAVAIISMVIGAVLGLTQTDVKRMVAYSSIAHAGFLLVGAIAMTKDGLSSTLFYLLAYGFTTLAAFGVISLVRDSSGEATHLSAWAGLAKRSPLVAGVFTFLLLALAGIPLTSGFVGKFVVFSAALSDGMAPLVVVALVFSAVAAFFYLRVIVLMYFSEPAADGPSVSVPGFGTGTAIFLGTGVTLVLGLVPAFALGWAGSGGFAF","length":522,"molWeight":54001,"crc64":"831D10A4ADD72104","md5":"8713CB72284E937F512F56B6BECE511E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":13,"Domain":1},"uniParcId":"UPI000B8B4FF7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SK89","uniProtkbId":"A0A229SK89_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-10-25","entryVersion":33,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59246.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NADH-quinone oxidoreductase subunit D"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NADH dehydrogenase I subunit D"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NDH-1 subunit D"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"nuoD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59246.1"}],"value":"CF165_48715"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005769"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003685"}],"value":"Belongs to the complex I 49 kDa subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59246.1"}],"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":175,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"NADH-quinone oxidoreductase subunit D","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00346"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000089","properties":[{"key":"ProteinId","value":"OXM59246.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954409.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000089.1"}]},{"database":"AlphaFoldDB","id":"A0A229SK89","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801496at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050136","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (quinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.10.645.10","properties":[{"key":"EntryName","value":"Cytochrome-c3 Hydrogenase, chain B"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01358","properties":[{"key":"EntryName","value":"NDH1_NuoD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001135","properties":[{"key":"EntryName","value":"NADH_Q_OxRdtase_suD"}]},{"database":"InterPro","id":"IPR014029","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_49kDa_CS"}]},{"database":"InterPro","id":"IPR022885","properties":[{"key":"EntryName","value":"NDH1_su_D/H"}]},{"database":"InterPro","id":"IPR029014","properties":[{"key":"EntryName","value":"NiFe-Hase_large"}]},{"database":"NCBIfam","id":"TIGR01962","properties":[{"key":"EntryName","value":"NuoD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004739","properties":[{"key":"EntryName","value":"PRK06075.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11993:SF10","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11993","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00346","properties":[{"key":"EntryName","value":"Complex1_49kDa"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56762","properties":[{"key":"EntryName","value":"HydB/Nqo4-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00535","properties":[{"key":"EntryName","value":"COMPLEX1_49K"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSTENLSDVTTGTSTTETGSDSTDSANYADSRDTTEGRVYTVSGGDWDDVIADAAHDERMVINMGPQHPSTHGVLRLVLEMEGETVTQLRSVIGYLHTGIEKNCEYRTWTQGVTFVTRMDYLAPLSTEMAYCLGVEKLLQIEAPRRAQLLRVMLLEINRIGSHLVYIATGGMELGATTAMTLGFREREEVLHLLEHLTGLRMNHAFIRPGGLAQDMPADYVEVVKAFIKTMKERLPLYDKLFTGQPIWRNRLKGVGYLPVDACLALGVTGPVLRSAGLPWDLRKTEPYSCYDEFEFDVPVDNGADCWSRYLIRVHEMHESLKIIEQCLEKLEPGPVMVEDKKVAWPAQLSIGSDGMGNSLEHVKKIMGQSMESLIHHFKLVTEGFKVPAGQVYTSVESPRGELGAHLVSDGGTRPLRVHVRDPSFVNLQSMPAMSEGGLVADVIAAIASIDPVMGGVDR","length":460,"molWeight":50765,"crc64":"94A43A20FF672DDC","md5":"637AEFFE56AD730CF9ACA1A8941A9D5A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI000B8AFFA4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SKB7","uniProtkbId":"A0A229SKB7_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Chromosome partition protein Smc"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59209.1"}],"value":"smc"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59209.1"}],"value":"CF165_48820"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Required for chromosome condensation and partitioning"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"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_01894"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Belongs to the SMC family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59209.1"}],"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":512,"modifier":"EXACT"},"end":{"value":626,"modifier":"EXACT"}},"description":"SMC hinge","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00968"}]},{"type":"Region","location":{"start":{"value":692,"modifier":"EXACT"},"end":{"value":719,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":814,"modifier":"EXACT"},"end":{"value":904,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":1005,"modifier":"EXACT"},"end":{"value":1039,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Compositional bias","location":{"start":{"value":692,"modifier":"EXACT"},"end":{"value":719,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023054"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000090","properties":[{"key":"ProteinId","value":"OXM59209.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954428.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000090.1"}]},{"database":"AlphaFoldDB","id":"A0A229SKB7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9808768at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005694","properties":[{"key":"GoTerm","value":"C:chromosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030261","properties":[{"key":"GoTerm","value":"P:chromosome condensation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007059","properties":[{"key":"GoTerm","value":"P:chromosome segregation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007062","properties":[{"key":"GoTerm","value":"P:sister chromatid cohesion"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03278","properties":[{"key":"EntryName","value":"ABC_SMC_barmotin"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000901","properties":[{"key":"EntryName","value":"Chromosome partition protein Smc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000984","properties":[{"key":"EntryName","value":"Chromosome partition protein Smc"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1060.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.1620","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01894","properties":[{"key":"EntryName","value":"Smc_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR003395","properties":[{"key":"EntryName","value":"RecF/RecN/SMC_N"}]},{"database":"InterPro","id":"IPR024704","properties":[{"key":"EntryName","value":"SMC"}]},{"database":"InterPro","id":"IPR010935","properties":[{"key":"EntryName","value":"SMC_hinge"}]},{"database":"InterPro","id":"IPR036277","properties":[{"key":"EntryName","value":"SMC_hinge_sf"}]},{"database":"InterPro","id":"IPR011890","properties":[{"key":"EntryName","value":"SMC_prok"}]},{"database":"NCBIfam","id":"TIGR02168","properties":[{"key":"EntryName","value":"SMC_prok_B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43977","properties":[{"key":"EntryName","value":"STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06470","properties":[{"key":"EntryName","value":"SMC_hinge"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02463","properties":[{"key":"EntryName","value":"SMC_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005719","properties":[{"key":"EntryName","value":"SMC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00968","properties":[{"key":"EntryName","value":"SMC_hinge"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75553","properties":[{"key":"EntryName","value":"Smc hinge domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MHLKSLTLKGFKSFASATTLRFEPGITCVVGPNGSGKSNVLDALRWVMGTQGAKDLRGGKMEDVIFAGTAGRAPLGRAEVTLTIDNADGALPIEYSEVSITRRMFRDGASEYEINGDRCRLMDVQELLSDSGIGREMHVIVGQGQLSAILESKPEERRAFIEEAAGVLKHRKRKEQTLRKLANMQGNLDRLGDLTTELRRQLKPLGKQAEIARKAQSVQSELRDSRLRLLADDLVTQRDAIAREEADEKTARARRAEVEQNLEIVSAEEAELEASLAEDAPLLQTAQETWYKLSALAERLRGTVRLAIERQRHLSADVSTNTGGRDPEELLEEAERVAEQEEELNEAVMEARELLAQTVLRREDLEQRVQAAERAHWAAVRAIADRREGMAKLTGQVEALRSKNGATSDEIDRLSVSLEEAAERAEIAVEELEMAKAEGGVEESDDAGLMDRHDRAVEANNAAKARVEELVKAERAAEREIASEKARVEALSMGLKRKDGAGALLGASHELPGLLGSVAALLTVEPGYEVALAAALGPVADAVAVTGGEDALRALKYLKDTDSGRAGILLGGPESTVDTYSWPSLPEGARWAREVVTAPAQLRPAVEQALDKLALVRDLDAARHLVAVHPEVRAVTAEGDVFGTRWAIGGSGKRESVIEVQAAVDEAAARLRTAERQLEQYAAELEGARAEQQARREEVSQAKDALGDAKVRKARSSERLNRMQQAARQAQAEVERLSGQRAKVEQSRVQALDQLAELEERLAAVAEQPVEDDPDTAERDQAVEELAVVRQEEMEARLAQRTAEERARSIAGKAEGLRRAAHAEQQARERAERAAAARKRGAEIANAVVNAGEIALERIEHSVQRAATERDQVQARRQSREQALTGVRAKVRELTGELEKLTDAVHRDEVLRAEQRLRLETLEAKIAEDFGIGLTDLVQEYGPDVPVPPSAGEMAEYEAAKDRGEDVTPPPPMPYDRDTQARRAKRAEKDLSLLGKVNPLALEEFAALEERYKFLSTQLEDLKDTRKDLEAVIKQVDEKILEVFASAYEDVAREFETVFGVLFPGGEGRMVLTEPDDLLSTGVDVEARPPGKKVKRLSLLSGGEKSLVAVGMLVAIFRARPSPFYVMDEVEAALDDTNMRRLIGLLEQLRDSSQLIIITHQKPTMEIADALYGVSMQGDGITKVISQRLRTTEEEPVPVG","length":1200,"molWeight":131657,"crc64":"73357214A2158563","md5":"0563622918D6079F9CE989A0FB2B53E7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Coiled coil":5,"Compositional bias":1,"Binding site":1},"uniParcId":"UPI000B8B303E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SKD2","uniProtkbId":"A0A229SKD2_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":33,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59286.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Protein translocase subunit SecA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"7.4.2.8"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"secA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59286.1"}],"value":"CF165_48560"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.","ecNumber":"7.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Distribution is 50-50"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004170"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004170"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007650"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"value":"Belongs to the SecA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59286.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":586,"modifier":"EXACT"}},"description":"SecA family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51196"}]},{"type":"Domain","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":592,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":501,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022927"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0653","category":"Biological process","name":"Protein transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023010"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0811","category":"Biological process","name":"Translocation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01382"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000088","properties":[{"key":"ProteinId","value":"OXM59286.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_093954382.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000088.1"}]},{"database":"AlphaFoldDB","id":"A0A229SKD2","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9805579at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031522","properties":[{"key":"GoTerm","value":"C:cell envelope Sec protein transport complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008564","properties":[{"key":"GoTerm","value":"F:protein-exporting ATPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0065002","properties":[{"key":"GoTerm","value":"P:intracellular protein transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0017038","properties":[{"key":"GoTerm","value":"P:protein import"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006605","properties":[{"key":"GoTerm","value":"P:protein targeting"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043952","properties":[{"key":"GoTerm","value":"P:protein transport by the Sec complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd17928","properties":[{"key":"EntryName","value":"DEXDc_SecA"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18803","properties":[{"key":"EntryName","value":"SF2_C_secA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000429","properties":[{"key":"EntryName","value":"Preprotein translocase subunit SecA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3060.10","properties":[{"key":"EntryName","value":"Helical scaffold and wing domains of SecA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"3.90.1440.10","properties":[{"key":"EntryName","value":"SecA, preprotein cross-linking domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01382","properties":[{"key":"EntryName","value":"SecA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR000185","properties":[{"key":"EntryName","value":"SecA"}]},{"database":"InterPro","id":"IPR026389","properties":[{"key":"EntryName","value":"SecA_Actinobact-type"}]},{"database":"InterPro","id":"IPR020937","properties":[{"key":"EntryName","value":"SecA_CS"}]},{"database":"InterPro","id":"IPR011115","properties":[{"key":"EntryName","value":"SecA_DEAD"}]},{"database":"InterPro","id":"IPR014018","properties":[{"key":"EntryName","value":"SecA_motor_DEAD"}]},{"database":"InterPro","id":"IPR011130","properties":[{"key":"EntryName","value":"SecA_preprotein_X-link_dom"}]},{"database":"InterPro","id":"IPR044722","properties":[{"key":"EntryName","value":"SecA_SF2_C"}]},{"database":"InterPro","id":"IPR011116","properties":[{"key":"EntryName","value":"SecA_Wing/Scaffold"}]},{"database":"InterPro","id":"IPR036266","properties":[{"key":"EntryName","value":"SecA_Wing/Scaffold_sf"}]},{"database":"InterPro","id":"IPR036670","properties":[{"key":"EntryName","value":"SecA_X-link_sf"}]},{"database":"NCBIfam","id":"TIGR04221","properties":[{"key":"EntryName","value":"SecA2_Mycobac"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30612:SF0","properties":[{"key":"EntryName","value":"CHLOROPLAST PROTEIN-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30612","properties":[{"key":"EntryName","value":"SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21090","properties":[{"key":"EntryName","value":"P-loop_SecA"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF07517","properties":[{"key":"EntryName","value":"SecA_DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01043","properties":[{"key":"EntryName","value":"SecA_PP_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07516","properties":[{"key":"EntryName","value":"SecA_SW"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00906","properties":[{"key":"EntryName","value":"SECA"}]},{"database":"SMART","id":"SM00957","properties":[{"key":"EntryName","value":"SecA_DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00958","properties":[{"key":"EntryName","value":"SecA_PP_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81886","properties":[{"key":"EntryName","value":"Helical scaffold and wing domains of SecA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF81767","properties":[{"key":"EntryName","value":"Pre-protein crosslinking domain of SecA"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01312","properties":[{"key":"EntryName","value":"SECA"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51196","properties":[{"key":"EntryName","value":"SECA_MOTOR_DEAD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAALISRVGKKLRRIIQRPGSVELTRYEALLPAVEKLEPELEKLSDEELTERAGKLRETLKDTAFGDDQLVEVCALGREAARRALGERAFDVQVLGTMGLLTKHVVQMETGEGKTLAGALAAAGYAIRGKRVHVVTVNDYLARRDAEWMGPVYTLLGVSVGWVEPSHSREERKEAYAKDVTYGAVAEIGFDVLRDRLVTKVDDLVQPPPEVAIVDEADSVLVDEARVPLVMAGSIDRSDADEEVAKIVRRLRLNLHYETDSEGRNAWLTDAGSSVVAKSLGIEVDDLFNEQASDRLAAVNVALHAHALLTRDVDYLVRDGKVQLINAARGRVAELQRWPDGLQAAVEAKEQVTATDHGEILDSITVQALLARYPEVAGMTGTAVAVAEQLREFYELEVAVIPPNTPNIREDLPDRVFASPSQKLRAIEEEIRTVHETGRPILVGTQDVAESEELAEKLAKVDLECVVLNARNDAEEAAIIAEAGKKGAVTVSTQMAGRGTDIRLGGTDGESREEVVELGGLHVIGTARYPSSRLDGQLRGRSGRQGDPGSAIFFASLNDELVLSNAPDVPEGITDDEETGEITDPAALRQLNHAQRVAEGVDLEIHRNTWRYTRLIERQRRDLLVHRDKVLRTAYAAEQLEKAHGEKFAELKERVDDQEKLEQVCREVLLFHVDQLWSDHLAYLTDVRESIHLRALARETPLDEFHRAAIPEFHKIIAEADSRAAKTLEEAELTDEGIDLGDAGVRRANTTWTYLVHDNPFDSDFEQTIKKVRSMIKRK","length":779,"molWeight":86224,"crc64":"3563ECF5C754B2E1","md5":"E9C078656374CC1923C419F8C42D25FF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Binding site":3},"uniParcId":"UPI000B8AC254"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SKE3","uniProtkbId":"A0A229SKE3_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59239.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"NADH-quinone oxidoreductase subunit K"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"NADH dehydrogenase I subunit K"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"NDH-1 subunit K"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"nuoK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59239.1"}],"value":"CF165_48680"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010519"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"value":"Belongs to the complex I subunit 4L family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59239.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}]},{"type":"Transmembrane","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}]},{"type":"Transmembrane","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01456"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000089","properties":[{"key":"ProteinId","value":"OXM59239.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003081840.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_NMUL01000089.1"}]},{"database":"AlphaFoldDB","id":"A0A229SKE3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92868329","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9810120at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030964","properties":[{"key":"GoTerm","value":"C:NADH dehydrogenase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050136","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (quinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042773","properties":[{"key":"GoTerm","value":"P:ATP synthesis coupled electron transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.10.287.3510:FF:000001","properties":[{"key":"EntryName","value":"NADH-quinone oxidoreductase subunit K"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.3510","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01456","properties":[{"key":"EntryName","value":"NDH1_NuoK"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001133","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_chain4L/K"}]},{"database":"InterPro","id":"IPR039428","properties":[{"key":"EntryName","value":"NUOK/Mnh_C1-like"}]},{"database":"NCBIfam","id":"NF004320","properties":[{"key":"EntryName","value":"nuoK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004321","properties":[{"key":"EntryName","value":"nuoK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11434:SF21","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE SUBUNIT 4L-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11434","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00420","properties":[{"key":"EntryName","value":"Oxidored_q2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTPTYYLLLSALLFALGAVGVLVRRNAIVVFMCIELMLNAVNLSLVTFARINGGLDGQIMAFFVMVVAAAEVVVGLAIIMAIFRTRRSASVDDTNLLKY","length":99,"molWeight":10743,"crc64":"E505E2458CE1AF43","md5":"9CFC3434672B8038841DB0263A5A777F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":3},"uniParcId":"UPI0001DB3F43"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A229SKE4","uniProtkbId":"A0A229SKE4_9PSEU","entryAudit":{"firstPublicDate":"2017-10-25","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-10-25","entryVersion":34,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis vastitatis","taxonId":1905142,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59415.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"ATP:glutamine synthetase adenylyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"ATase"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Glutamine synthetase adenylyl-L-tyrosine phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"2.7.7.89"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Adenylyl removase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AR"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AT-N"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Glutamine synthetase adenylyl transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"2.7.7.42"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Adenylyl transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AT-C"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"glnE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59415.1"}],"value":"CF165_47590"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18589"},{"database":"Rhea","id":"RHEA-COMP:10660"},{"database":"Rhea","id":"RHEA-COMP:10661"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"}],"ecNumber":"2.7.7.42","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43716"},{"database":"Rhea","id":"RHEA-COMP:10660"},{"database":"Rhea","id":"RHEA-COMP:10661"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.7.89","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Belongs to the GlnE family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OXM59415.1"}],"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":88,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Glutamate-ammonia ligase adenylyltransferase repeated","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03710"}]},{"type":"Domain","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08335"}]},{"type":"Domain","location":{"start":{"value":588,"modifier":"EXACT"},"end":{"value":822,"modifier":"EXACT"}},"description":"Glutamate-ammonia ligase adenylyltransferase repeated","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03710"}]},{"type":"Domain","location":{"start":{"value":848,"modifier":"EXACT"},"end":{"value":989,"modifier":"EXACT"}},"description":"PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08335"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"Adenylyl removase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]},{"type":"Region","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":992,"modifier":"EXACT"}},"description":"Adenylyl transferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"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_00802"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DR8TPC01B71Q9","citationType":"submission","authors":["Adamek M.","Alanjary M.","Sales-Ortells H.","Goodfellow M.","Bull A.T.","Kalinowski J.","Ziemert N."],"title":"Comparative genome mining reveals phylogenetic distribution patterns of secondary metabolites in Amycolatopsis.","publicationDate":"JUL-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}],"value":"H5","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000215199"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"NMUL01000083","properties":[{"key":"ProteinId","value":"OXM59415.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A229SKE4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9759366at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000215199","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:0008882","properties":[{"key":"GoTerm","value":"F:[glutamate-ammonia-ligase] adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0047388","properties":[{"key":"GoTerm","value":"F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase 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:0062132","properties":[{"key":"GoTerm","value":"P:regulation of L-glutamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05401","properties":[{"key":"EntryName","value":"NT_GlnE_GlnD_like"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.460.10","properties":[{"key":"EntryName","value":"Beta Polymerase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.20.120.330","properties":[{"key":"EntryName","value":"Nucleotidyltransferases domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00802","properties":[{"key":"EntryName","value":"GlnE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023057","properties":[{"key":"EntryName","value":"GlnE"}]},{"database":"InterPro","id":"IPR005190","properties":[{"key":"EntryName","value":"GlnE_rpt_dom"}]},{"database":"InterPro","id":"IPR043519","properties":[{"key":"EntryName","value":"NT_sf"}]},{"database":"InterPro","id":"IPR013546","properties":[{"key":"EntryName","value":"PII_UdlTrfase/GS_AdlTrfase"}]},{"database":"NCBIfam","id":"NF010707","properties":[{"key":"EntryName","value":"PRK14109.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30621:SF0","properties":[{"key":"EntryName","value":"BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30621","properties":[{"key":"EntryName","value":"GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08335","properties":[{"key":"EntryName","value":"GlnD_UR_UTase"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF03710","properties":[{"key":"EntryName","value":"GlnE"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF81301","properties":[{"key":"EntryName","value":"Nucleotidyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF81593","properties":[{"key":"EntryName","value":"Nucleotidyltransferase substrate binding subunit/domain"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MMADRARTTASAARYGFTDARAEGQLRTAGWWDDGGPVASATDVLSALSRTADPDLALRGLDRIREADAGEWAPLAEQLCANRTFRGRLLSVLGTSSALADFVAANPEQWRSLTGDKCTDAACYREALRAALLGDDGSVLTGLKAEQALKVAYRGQLLGIAAADLGHVVEPGLEHPRYAEVAAQLTELAEAALAAGLVVAEAEVGAAADGTLAIIAMGKCGGRELNYVSDVDVIFVGEGDLGAATRLASTMMRVVGKACFEVDAALRPEGKAGALVRTVESHHGYYQKWAKTWEFQALLKARPVAGDAELGRQYAEMVAPLVWSAADRENFVGEVQQMRRRVEGHVPSEHAERELKLGRGGLRDVEFAVQLLQLVHGRIDANLRSPSTMDALAALGEGGYVGRQDAAELGASYEFLRMIEHRLQLRRLRRTHLFPATSETGELRILARASGIKASGGKSQGDALLAEFRRHGKGVRRLHEKIFYRPLLQSVANVPTEALRLTTKQAASRLAALGYTAPDGALQHIKALTSGVSRRAAIQQALLPVLLDLFADTPDPDGGLLSYRKVSEALEDTPWYLRVLRDEGTVVENLALLLGTSRLVPDLLVRAPEVLQLLGDPARLLGRTPAEVATSLRAAVRRQPGLNAAVAAARSLRRHELLRVACADLLGLLDVPAVCEALSSVWVAVLQGALAAAFRQRQAELGRTPARIAVIGMGRLGGAELGYGSDADVLFVCEPSEGVSDADAVKFASSVAETVRKMLGAPSSDPALVVDADLRPEGRSGPLVRTLDSYRAYYARWGEVWEAQALLRARFIAGDDELGGRFIAMIDPIRYPEGGLAAKDAREVRRIKARVETERMPRGADPTRHTKLGRGGLADVEWTVQLLQLQHAHAVPALRTTSTLDALACLPEAGLAEQAQVDSLREAWLLATQVRNAGMLVRGKAVDEVPGSGRDLAAVARVLGQTAGDDPGEFLDTYRRITRRAHTVVEHLFYEA","length":992,"molWeight":106621,"crc64":"5B039C292382826C","md5":"05A8920F6372D2BF8A79FDF2663D25DC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":4,"Region":2},"uniParcId":"UPI000B8AB964"}}]}