{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N867","uniProtkbId":"A0ABP9N867_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111699.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5111699.1"}],"value":"GCM10023320_04950"}]}],"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":"GAA5111699.1"}],"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":"UP001500804"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000002","properties":[{"key":"ProteinId","value":"GAA5111699.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345602922.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000002.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MRVGVLTGGGDCPGLNAVIRAIVRKGVPEYGYSFLGFRDGWRGPLEALTRPLDIPAVRGLLPRGGTILGSSRTNPFAVEGGVEKIRRNLQNLGVDALIAIGGEDTLGVATKLHETGVNVVGVPKTIDNDLNGTDYTFGFDTAVNIATEAIDRLHTTAESHHRALIVEVMGRHAGWIALHSGMAGGANAILIPEVRFDLDQVCQWVEARFQLDYAPIIVVAEGAMPKEGEEVLQSGEKDAFGHVRLGGIGDWLAHRIEERTGKEARTTVLGHVQRGGTPTARDRWLATRFGLHAIDAVHAGKWGQMTALRGTDVVTVPLSEATKELKVVDPGLYAEAEVFFG","length":341,"molWeight":36574,"crc64":"895D27D424102CEA","md5":"E4DE461AD8EEFC48C2023410048F778C"},"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":"UPI0031E81893"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9ND85","uniProtkbId":"A0ABP9ND85_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5115051.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate dehydrogenase [ubiquinone]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"1.2.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate oxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"POX"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate:ubiquinone-8 oxidoreductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5115051.1"}],"value":"poxB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5115051.1"}],"value":"GCM10023320_13210"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + pyruvate + H2O = a ubiquinol + acetate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27405"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:30089"}],"ecNumber":"1.2.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362132"}],"value":"Belongs to the TPP enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5115051.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00205"}]},{"type":"Domain","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]},{"type":"Region","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"FAD-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Region","location":{"start":{"value":531,"modifier":"EXACT"},"end":{"value":572,"modifier":"EXACT"}},"description":"Membrane-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"Moves into active site upon enzyme activation, plays a role in electron transfer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5115051.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5115051.1"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000004","properties":[{"key":"ProteinId","value":"GAA5115051.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345603896.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000004.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008289","properties":[{"key":"GoTerm","value":"F:lipid binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052737","properties":[{"key":"GoTerm","value":"F:pyruvate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048039","properties":[{"key":"GoTerm","value":"F:ubiquinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042867","properties":[{"key":"GoTerm","value":"P:pyruvate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02014","properties":[{"key":"EntryName","value":"TPP_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07039","properties":[{"key":"EntryName","value":"TPP_PYR_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00850","properties":[{"key":"EntryName","value":"POX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR047211","properties":[{"key":"EntryName","value":"POXB-like"}]},{"database":"InterPro","id":"IPR044261","properties":[{"key":"EntryName","value":"Pyruvate_dehydrogenase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012000","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_cen_dom"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"InterPro","id":"IPR047212","properties":[{"key":"EntryName","value":"TPP_POXB-like"}]},{"database":"InterPro","id":"IPR047210","properties":[{"key":"EntryName","value":"TPP_PYR_POXB-like"}]},{"database":"NCBIfam","id":"NF006591","properties":[{"key":"EntryName","value":"poxB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981:SF2","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00205","properties":[{"key":"EntryName","value":"TPP_enzyme_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTTVAEQIVRTLQANGVQRVYGIPGDSLNGFTDALRKDGRIRWLHVRHEEAAAFAAAAEAATTGRLAVAAGSCGPGNLHLINGLYDANRSRVPVLAIAAHIPTGEIGSGYFQETRPQELFREASVYSEYVADASQMPQVLEIAMRTAISRCGVAVVVIPGDVALSAARSQPTASIRSTTPVVVPAESELREAADVLNGGSRVTILAGAGVAGAHDEVTAIADALGAPIVHTLRGKEFIEHDNPCDVGMTGLLGFASGYRAMSRAQTLLMLGTDFPYRQFYPAHATTIQVDLRGEQLGRRHPVDLGLVGTVKDTAAALLPMLDRKTDRRHLDDARDHYRRTRAKLDELATPSRNNAPIHPQYLARLVDQHAADDAVFVPDVGSPVVWAARYLTMNGRRRLIGSFVHGSMANALPHAIGAQAAHAGRQVVALSGDGGLTMLLGELITLTQNRLPVKVIVFNNSSLNFVELEMKAAGFVNFGTDLINPDFAEVARAMGIHGRRVERSADLPAAVKEILDHDGPALLDVVTERQELTIPPAITAEQMKGFTLYALHTVMSGRGDELIDLAKANLRQLF","length":574,"molWeight":61606,"crc64":"06B63C24000E1A22","md5":"32737BCEBA347A76C53EAD99A91749FB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":9,"Site":1},"uniParcId":"UPI0031EDFB7F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NGV0","uniProtkbId":"A0ABP9NGV0_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5119459.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5119459.1"}],"value":"GCM10023320_25220"}]}],"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":"GAA5119459.1"}],"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":20,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":25,"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":110,"modifier":"EXACT"},"end":{"value":116,"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":152,"modifier":"EXACT"},"end":{"value":153,"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":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"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":401,"modifier":"EXACT"},"end":{"value":404,"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":455,"modifier":"EXACT"},"end":{"value":455,"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":459,"modifier":"EXACT"},"end":{"value":459,"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":219,"modifier":"EXACT"},"end":{"value":219,"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":"GAA5119459.1"}],"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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000008","properties":[{"key":"ProteinId","value":"GAA5119459.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001500804","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":"MPLDVLGAAIGVAASGPATVTGVTLRASDARHGDLFAALPGTRAHGADYAAVAVAGGAVAVLTDPAGARRPALAGVPLLVHPHPREVLGALAALVHGDPTAHLRVLGVTGTSGKTTTAHLLEAGLAAAGRATGLLGTVGTHIRGSRLPAALTTPEAPDLQALFAVMAEDGVTDVAMEVSSHALAMGRVAGTRFAVAAFTNLSQDHLDFHRDMEDYFEAKAALFDGRAEHAVVCVDDEWGRRLAARTPGAVTVSTGGPAAWRGVDVHTGPDGTQSFTAVAPDGAQLPVRLQLPGAFNVANAVVALACLDAAGVPAAVAAEGFAGVAVPGRMQRIEQGQPFLAIVDYAHKPGAVAALLDALRPQVPGRLIVVLGCGGDRDRGKRPVMGAAAAARAELLIVTDDNPRTEDPAGIRAEMLAGARAEPGAGDLMEIGDRRAAIAAAVASAKPGDAVVVAGKGHETGQEVAGVKHPFDDAAEVAAALGAALQGTR","length":489,"molWeight":49096,"crc64":"05A671F8E597CF8D","md5":"F02660F2C6DF6A0EFD59B81D330316AD"},"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":"UPI0031E77A3A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NH97","uniProtkbId":"A0ABP9NH97_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5120082.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"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:0000313","source":"EMBL","id":"GAA5120082.1"}],"value":"katG_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"katG"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5120082.1"}],"value":"GCM10023320_26840"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5120082.1"}],"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":111,"modifier":"EXACT"},"end":{"value":430,"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":39,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":750,"modifier":"EXACT"},"end":{"value":777,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":750,"modifier":"EXACT"},"end":{"value":761,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":768,"modifier":"EXACT"},"end":{"value":777,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"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":273,"modifier":"EXACT"},"end":{"value":273,"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":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-109)","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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000008","properties":[{"key":"ProteinId","value":"GAA5120082.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345605308.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000008.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.520.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"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":"MTDVQSPGTPVDEKSGGGLGLPAPAPPRSRPRRPTTNRDWWPHQLDLSILRKHPAAADPMGPDFDYAAEFATLDLDALARDIDEVLTTSQDWWPADFGHYGPLVVRMVWHCAGTYRVGDGRGGPGAGTQRFAPLNSWPDNRNLDKARRLLWPVKEKYGRKISWADLMVFAGNRALESMGFTTFGFGGGRVDVWEPEEDVYWGPEHAWLGDERHTGVRDLERPLAADQMGLIYVNPEGPNTVPDPFTSARDIRHTFRRMGFDDEETVALIAGGHSFGKAHGAGDPERLLGPDPEAAPIEDQGLGWRCGHGTGKGPDTISSGLEGTWTATPTRWDNSFFENLFEFEWDLELSPGDLWQWLPRDGGGAGTVPDAHDPSKAHPPKILTTDLALRFDPIYEPIARRFYENPDQMADAFARVWFKLTHIDMGPIQRYLGPLVPRESLIWQDPVPAVDHELVDADDVAALKAQVLASGLSVSQLVSTAWASASTFRTSDKRGGANGARIRLEPQRDWEVNEPDELARVLRTLEGVRESFNGGQAGGKKISLADLIVLGGCAAVEQAARDAGHDVRVPFTPGRTDASQDRTDVEWFAPLEPVADGFRNYRGKGGRVPSEHLLVDRANLLDLSAPEMTVLVGGLRVLGANHRRSPLGVLTSAPGTLTNDFFRNLLDMGTTWKPTSKGAETFEGRDRASGEVRWTASRVDLVFGSHSELRAIAEVYASRDGRERFVRDFVAAWDKVMNLDRYDIRRWPAGRCRRPGAAAPPGRGGRPAGSAPRAPRR","length":777,"molWeight":85553,"crc64":"66760CB834BC4B25","md5":"1B2F940ED2EAC925B34B41625AEFBEB9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI0031F0BBB9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NK17","uniProtkbId":"A0ABP9NK17_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5123566.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5123566.1"}],"value":"GCM10023320_35450"}]}],"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":"GAA5123566.1"}],"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":458,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Domain","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":610,"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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000012","properties":[{"key":"ProteinId","value":"GAA5123566.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345606217.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000012.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MGHFRSNLRDLEFNLFEVFRVQDRLGTAPFDGVDEDTVRGVLTELNAVATGPLADSFADADRNPPVFDPATHSVTLPQSFKDSYRALWDGEWWRISLPADLGGYGIPATVQWAASELILGANPAVFMYMAGPNFAAVVHRNGTEQQKRWAEIMIDRGWGATMVLTEPDAGSDVGAGRTKAVQQADGTWHIEGVKRFITSGEHDLTENIMHLVLARPEGPGITPRPGTKGLSLFLVPKFHFDPETGEPGERNGAFVTGVEHKMGLKASTTCELTFGQHGVPAVGWLLGEVHDGIAQMFQVIEYARMMVGTKAIGTLSAGYLAALEYAKDRVQGADLTRQLDKTAPRVTITHHPDVRRILMLQKAYAEGLRALYTYTATFQDQVKAGAATGADTTLAERVNDLLLPIVKGVGSERASEQLLLSLQTLGGSGYLQDYPIEQYIRDAKIDSLYEGTTAIQSMDFLFRKIVRDNGQAIGHVAGEIQAFLDAESGNGRLKEERALLATALTDVQGMLGALTGFLMASAEDPTSLYKVGQNTVRLLMAVGDLLIGWLLLRQAEVALTALGGEPSARDVAFYEGKVGAARFFAKTVLPQLTAQRAIVEATDNSLMELPEAAF","length":614,"molWeight":66595,"crc64":"BA4A83887F206478","md5":"91B752A94AE96DF146C7D8B87D701432"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":9,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0031E84EAB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NMC7","uniProtkbId":"A0ABP9NMC7_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5125297.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5125297.1"}],"value":"GCM10023320_39520"}]}],"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":"GAA5125297.1"}],"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":275,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":541,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":522,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"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":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"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":17,"modifier":"EXACT"},"end":{"value":17,"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":18,"modifier":"EXACT"},"end":{"value":23,"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":75,"modifier":"EXACT"},"end":{"value":75,"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":75,"modifier":"EXACT"},"end":{"value":75,"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":149,"modifier":"EXACT"},"end":{"value":149,"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":156,"modifier":"EXACT"},"end":{"value":158,"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":196,"modifier":"EXACT"},"end":{"value":201,"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":196,"modifier":"EXACT"},"end":{"value":201,"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":232,"modifier":"EXACT"},"end":{"value":232,"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":232,"modifier":"EXACT"},"end":{"value":232,"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":250,"modifier":"EXACT"},"end":{"value":250,"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":363,"modifier":"EXACT"},"end":{"value":363,"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":391,"modifier":"EXACT"},"end":{"value":394,"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":414,"modifier":"EXACT"},"end":{"value":414,"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":475,"modifier":"EXACT"},"end":{"value":475,"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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000014","properties":[{"key":"ProteinId","value":"GAA5125297.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345606671.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000014.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQPRATRHLFVTGGVASSLGKGLTASSLGQLLTARGLRVIMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDIGHYERFLDRNLHGRANVTTGQVYSSVIAKERRGEYLGDTVQVIPHITNEIKDRIRAMAEPDDDGIVPDVVITEVGGTVGDIESLPFLEAVRQVRHDVGRDNCFFLHVSLVPYLAPSGELKTKPTQHSVAALRNIGIQPDALVLRADREIPDGLKRKISLMCDVDTDGVVAAPDAPSIYDIPRVLHREGLDAYVVRRLGLPFRDVDWTVWGDLLDRVHHPDETVRIALVGKYVDLPDAYLSVTEALRAGGFAHRARVEIVWVQSDECRTPAGAAAHLEGMDGVLIPGGFGVRGIEGKLGAIRHARTRGIPTLGLCLGLQCMVIEAARSLGGLADANSSEFDERTPHPVISTMADQRDVVAGERDMGGTMRLGAYPAVLKKGSVVAGAYGAREVSERHRHRYEVNNSYRERLEGVGLVFGGTSPDGKLVEFIELPTDAHPFFVGTQAHPELKSRPTRPHPLFAAFVKAALAYRAADRLPVELPAREPATAGAKAGVNGAAS","length":575,"molWeight":62268,"crc64":"E9A803181A7FC5D2","md5":"82A6A3E294AD13CDAC2351DFEB73B343"},"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":"UPI0031EB293C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NN84","uniProtkbId":"A0ABP9NN84_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128462.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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:0000313","source":"EMBL","id":"GAA5128462.1"}],"value":"katG_2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"katG"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128462.1"}],"value":"GCM10023320_47410"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128462.1"}],"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":132,"modifier":"EXACT"},"end":{"value":407,"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":29,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":364,"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":"Active site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"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":261,"modifier":"EXACT"},"end":{"value":261,"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":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-98)","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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000018","properties":[{"key":"ProteinId","value":"GAA5128462.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345607498.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000018.1"}]},{"database":"Proteomes","id":"UP001500804","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":"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":"MTESISETENPSIPSPTPEVTRPRTNRDWWPNQPDLTVLHQHSARANPLGADFDYAEAFSTLDVEELKRDVVEVMRTSQDWWPADYGHYGPLFIRMSWHSAGTYRIHDGRGGGGQGAQRFAPLNSWPDNASLDKARRLLWPVKEKYGRKISWADLLVFAGNVAIEDMGLPTFGFAFGREDIWQPEEIFWGSEDTWLGDERYSGERDLAEPFGAVQMGLIYVNPEGPNGNPDPLASARDIRETFKRMAMNDEETVALIVGGHTFGKCHGAVDPQYIGPEPEACPVEHQGIGWKNRVGTGAGPHAMTSGLEGAWTTAPTTWDNGYLDNLYGYDWELTRSPAGAHQWTPKNPEAQGTVPDAHDPSKRHAPMMLTSDIGLKVDPIYGPITKRFHENPAELADAFARAWYKLLHRDMGPVSRYLGPWVPEPQLWQDPVPAVDHELIGDAEIAALKEKVLASGLSVSQLVSTAWASAASFRGTDKRGGANGARIRLAPQKDWEVNNPDELGEVLQTLEQIQRDFNSTQAAKRVSLADLIVLGGGAAVEKAAKDAGHEVTVPFAPGRTDASQEQTDVDSFAVLEPKADGFRNYLRAGEKLPPETLLVDRAYMLTLSAPEMTVLVGGMRALNANVGQSAHGVFTDRPGTLTNDFFRNLLDMRTEWRVSDAENVYEGRDRATGELRWTATAADLVFGSNSQLRAIAEVYASADAKEKFVRDFAAAWDKVMNLDRFDLR","length":729,"molWeight":80605,"crc64":"ED309A65F671912D","md5":"B3008C4167B047FE0FDC099D14388923"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI0031E8BE1B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NNP3","uniProtkbId":"A0ABP9NNP3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128999.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5128999.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128999.1"}],"value":"GCM10023320_48910"}]}],"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":"GAA5128999.1"}],"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":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":870,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":952,"modifier":"EXACT"},"end":{"value":1097,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":952,"modifier":"EXACT"},"end":{"value":1099,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"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":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"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":210,"modifier":"EXACT"},"end":{"value":210,"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":241,"modifier":"EXACT"},"end":{"value":241,"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":242,"modifier":"EXACT"},"end":{"value":242,"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":243,"modifier":"EXACT"},"end":{"value":243,"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":285,"modifier":"EXACT"},"end":{"value":285,"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":285,"modifier":"EXACT"},"end":{"value":285,"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":285,"modifier":"EXACT"},"end":{"value":285,"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":299,"modifier":"EXACT"},"end":{"value":299,"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":299,"modifier":"EXACT"},"end":{"value":299,"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":299,"modifier":"EXACT"},"end":{"value":299,"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":299,"modifier":"EXACT"},"end":{"value":299,"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":299,"modifier":"EXACT"},"end":{"value":299,"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":301,"modifier":"EXACT"},"end":{"value":301,"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":301,"modifier":"EXACT"},"end":{"value":301,"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":715,"modifier":"EXACT"},"end":{"value":715,"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":754,"modifier":"EXACT"},"end":{"value":754,"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":756,"modifier":"EXACT"},"end":{"value":756,"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":761,"modifier":"EXACT"},"end":{"value":761,"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":786,"modifier":"EXACT"},"end":{"value":786,"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":787,"modifier":"EXACT"},"end":{"value":787,"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":788,"modifier":"EXACT"},"end":{"value":788,"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":789,"modifier":"EXACT"},"end":{"value":789,"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":829,"modifier":"EXACT"},"end":{"value":829,"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":829,"modifier":"EXACT"},"end":{"value":829,"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":829,"modifier":"EXACT"},"end":{"value":829,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":843,"modifier":"EXACT"},"end":{"value":843,"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":843,"modifier":"EXACT"},"end":{"value":843,"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":"UP001500804"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000019","properties":[{"key":"ProteinId","value":"GAA5128999.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345607639.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000019.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MPRRDDIRHVMVIGSGPIVIGQAAEFDYSGTQACRVLRAEGLRVSLVNSNPATIMTDPEFADATYVEPVTPEFLEQVIAAERPDAILPTLGGQTALNAAVALHESGVLERYGVELIGADIDAIQRGEDRLKFKEIVQSVGGDVPRSAVCHSMDEVRAAAADLGLPVVIRPSFTMGGLGSGMAHTPEDLERLASTGLAASPVTEVLIEESVLGWKEYELELMRDKHDNVVVVCSIENLDPMGVHTGDSITVAPAMTLTDREYQRMRDVGIAVLRAVGVDTGGCNIQFAVHPGTGRLVVIEMNPRVSRSSALASKATGFPIAKIAARLAIGYTLDEIRNDITGETPAAFEPTLDYVVVKIPRFAFEKFPGADPELTTTMKSVGEAMALGRSFQEALGKALRSMETSRVGFWTALDPDGDPDVAASREGRIYAVEQALRMGRSVADVAAESGIDPWFLDQILGLTELRQEIEDAAVLDAPLLRRAKRAGLSDRQIAVLRPEFAGEDGVRSLRHRLGIRPVYKTVDTCAAEFAARTPYHYSAYETDPAAESEIAPQTEKPKVLILGSGPNRIGQGIEFDYSCVHAVMALREAGFETVMVNCNPETVSTDYDTADRLYFEPLTFEDVLEVVHAEQVSGTVAGVIVQLGGQTPLGLAQRLTAAGVPVVGTSAAAIDLAEDRGAFGEVLRKAGLPAPAFGMATSFDEARAIAARIGYPVLVRPSYVLGGRGMEIVYDDETLAGYISRATTISEDRPVLVDRFLDDAIEIDVDALCDGSEVFIGGVMEHIEEAGVHSGDSSCALPPITLGRSVLEQVRRSTEAIAHGVGVRGLLNVQYALHGETLYVLEANPRASRTVPFVSKATAVPLAKAAARIMLGATIAELRAEGLLPGHGDGGELPPDAPIAVKEAVLPFHRFRTVEGHGVDPLLGPEMKSTGEVMGFDASFGAAFAKSQAGAYGSLPTSGRVFVSMADRDKRAMVFPVLRLADLGFEVLATEGTADVLRRHGVAATVVRKHSDGSTEGGETIVDRILAGDVDLIINTPYGNSGPRVDGYEIRSAAVARGVPCITTVQGAGAAVQGIEAMKAGRIGVRSLQDAHASLLKARS","length":1099,"molWeight":116833,"crc64":"4FA5A6FAC88D7AD9","md5":"46FF1CBCB4921D753D7E510E58F329AB"},"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":"UPI0031EDC17A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NNU5","uniProtkbId":"A0ABP9NNU5_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5129079.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5129079.1"}],"value":"GCM10023320_49110"}]}],"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":"GAA5129079.1"}],"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":225,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"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":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":43,"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":43,"modifier":"EXACT"},"end":{"value":43,"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":43,"modifier":"EXACT"},"end":{"value":43,"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":47,"modifier":"EXACT"},"end":{"value":47,"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":155,"modifier":"EXACT"},"end":{"value":159,"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":158,"modifier":"EXACT"},"end":{"value":158,"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":179,"modifier":"EXACT"},"end":{"value":179,"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":273,"modifier":"EXACT"},"end":{"value":277,"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":278,"modifier":"EXACT"},"end":{"value":278,"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":289,"modifier":"EXACT"},"end":{"value":289,"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":294,"modifier":"EXACT"},"end":{"value":294,"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":317,"modifier":"EXACT"},"end":{"value":319,"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":339,"modifier":"EXACT"},"end":{"value":339,"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":374,"modifier":"EXACT"},"end":{"value":374,"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":379,"modifier":"EXACT"},"end":{"value":379,"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":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"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":"UP001500804"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000019","properties":[{"key":"ProteinId","value":"GAA5129079.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345607656.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000019.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MSAGVDGEAARPVTPGGFESIERAVADLRAGKAIVVVDDEDRENEGDLIFAAEMATPELVSFMVRYTSGYICVPLTESECDRLDLPPMHHTNADSFRTAFTVTVDAKAGVTTGISAADRAHTIRLLADPSTGPGDLVRPGHILPLRAREGGVLRRPGHTEAAVDLARLAGLRPAGVLCEIVSQKDVGDMARADELQVFAEEHDLTLITIADLIAYRRRYEKHVVRVAQARIPTAHGDFIAYGYDSLLDGIEHIAMVRGDVATPESTGEDVLVRVHSECLTGDVMGSLRCDCGPQLDAALAAVAAEGRGVVLYMRGHEGRGIGLLHKLQAYQLQEAGADTVDANLALGLPADARDYGTGAQILADLGIKSMRLLTNNPDKRAGLEGYGLTITGRVPLPVRAHRENLRYLRTKRDRMGHDLPDLGEALADSTGS","length":432,"molWeight":46260,"crc64":"4FEBA664A57ED560","md5":"32FA841B643D3310CB607E1444A4A659"},"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":"UPI0031EE026C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NNZ0","uniProtkbId":"A0ABP9NNZ0_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5127793.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013120"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Aspartate-semialdehyde dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"ASA dehydrogenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"ASADH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013120"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"1.2.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Aspartate-beta-semialdehyde dehydrogenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"asd"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5127793.1"}],"value":"GCM10023320_45670"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate 4-semialdehyde + phosphate + NADP(+) = 4-phospho-L-aspartate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24284"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57535"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"1.2.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047891"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005076"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005021"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005097"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010584"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Belongs to the aspartate-semialdehyde dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5127793.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Semialdehyde dehydrogenase NAD-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00859"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000148-1"}]},{"type":"Active site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000148-1"}]},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:43474"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"phosphate","id":"ChEBI:CHEBI:43474"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022915"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0220","category":"Biological process","name":"Diaminopimelate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022697"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02121"}],"id":"KW-0791","category":"Biological process","name":"Threonine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000017","properties":[{"key":"ProteinId","value":"GAA5127793.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345607315.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000017.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0004073","properties":[{"key":"GoTerm","value":"F:aspartate-semialdehyde dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046983","properties":[{"key":"GoTerm","value":"F:protein dimerization activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0071266","properties":[{"key":"GoTerm","value":"P:'de novo' L-methionine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:1901705","properties":[{"key":"GoTerm","value":"P:L-isoleucine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009085","properties":[{"key":"GoTerm","value":"P:L-lysine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009088","properties":[{"key":"GoTerm","value":"P:L-threonine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd18131","properties":[{"key":"EntryName","value":"ASADH_C_bac_euk_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02316","properties":[{"key":"EntryName","value":"VcASADH2_like_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02121","properties":[{"key":"EntryName","value":"ASADH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012080","properties":[{"key":"EntryName","value":"Asp_semialdehyde_DH"}]},{"database":"InterPro","id":"IPR005986","properties":[{"key":"EntryName","value":"Asp_semialdehyde_DH_beta"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR000534","properties":[{"key":"EntryName","value":"Semialdehyde_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR012280","properties":[{"key":"EntryName","value":"Semialdhyde_DH_dimer_dom"}]},{"database":"NCBIfam","id":"TIGR01296","properties":[{"key":"EntryName","value":"asd_B"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011456","properties":[{"key":"EntryName","value":"PRK14874.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46278:SF2","properties":[{"key":"EntryName","value":"ASPARTATE-SEMIALDEHYDE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46278","properties":[{"key":"EntryName","value":"DEHYDROGENASE, PUTATIVE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01118","properties":[{"key":"EntryName","value":"Semialdhyde_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02774","properties":[{"key":"EntryName","value":"Semialdhyde_dhC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000148","properties":[{"key":"EntryName","value":"ASA_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00859","properties":[{"key":"EntryName","value":"Semialdhyde_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDEFAHEQHGRHEHGRHERGPVLALVGATGAVGTTMIEIIDARPDVPWSDIRLVASPRSAGKVLRVRGVDTTVQALAPEVFDGVDVALFDVPDEVSAQWAPIAAERGAVAVDNSGAFRMDPDVPLVVPEVNAEKAAERPKGIIANPNCTTLSMMAAMGALHREFGLEALVVASYQAASGAGQGGIDRLYAELSAVAGRQVGVQGGDVAAALAAAGLDAAASPFPAPLALNVVPWAGSLKDDGWSSEELKVRNEARKILGIPDLKVSATCVRVPVVTTHSLAVHAMFSREVPVEAARKVLAEQPSIVLRDDAAAGEFPTPAEAVGSDPTWVGRIRQALDFPNTLELFVCGDNLRKGAALNTYEIAETVAISL","length":372,"molWeight":38985,"crc64":"ACFC5835BD187D89","md5":"4575D07023985BBA65C470C840C23FA0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":2,"Binding site":7},"uniParcId":"UPI0031E78C27"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NP17","uniProtkbId":"A0ABP9NP17_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5129019.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5129019.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5129019.1"}],"value":"GCM10023320_48970"}]}],"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":"GAA5129019.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":325,"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":343,"modifier":"EXACT"},"end":{"value":343,"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":347,"modifier":"EXACT"},"end":{"value":347,"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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000019","properties":[{"key":"ProteinId","value":"GAA5129019.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345607642.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000019.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MSPRVLLGVAGGIAAYKSAELLRRLTETGHSVRVLPTPSALEFVGAATFEALSGRPVHTGVFSDVPEVPHVRLGQEAELVVVAPATADLMARAAAGRADDLLTASLLTARCPVLFAPAMHTEMWEHPATRANVELLRSRGVVVMEPASGRLTGADTGPGRLPDPAEIAELARLLLERGDALPRDLAGRRVVVSAGGTREALDPVRYLGNRSSGRQGYALARVAAQRGAHVTLVAAHTADLGDPAAVDVVRVGSALELRDAMHAAAKGADAVVMAAAVADFRPDTLAAHKIKKDGSEPPPLRLALNPDILVELVGAREPGQIVVGFAAETGDASGDPLHHGRAKLARKGCDLLVVNAVGDGRAFEVPDNAGWLLGADGTERELESGSKALLASHVWDAVAARLG","length":403,"molWeight":41836,"crc64":"5BEE81AD2A418913","md5":"E4D6F0875D2AB22E83408A1248E74E66"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI0031EB58EE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NQC3","uniProtkbId":"A0ABP9NQC3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5130991.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"RecBCD enzyme subunit RecB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"3.1.11.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"DNA 3'-5' helicase subunit RecB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Exonuclease V subunit RecB"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"ExoV subunit RecB"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Helicase/nuclease RecBCD subunit RecB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5130991.1"}],"value":"recB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5130991.1"}],"value":"GCM10023320_53630"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.","ecNumber":"3.1.11.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Belongs to the helicase family. UvrD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5130991.1"}],"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":331,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51198"}]},{"type":"Domain","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":622,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51217"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"DNA-binding and helicase activity, interacts with RecC","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":784,"modifier":"EXACT"},"end":{"value":1107,"modifier":"EXACT"}},"description":"Nuclease activity, interacts with RecD and RecA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Active site","location":{"start":{"value":995,"modifier":"EXACT"},"end":{"value":995,"modifier":"EXACT"}},"description":"For nuclease activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00560"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":851,"modifier":"EXACT"},"end":{"value":851,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":981,"modifier":"EXACT"},"end":{"value":981,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":995,"modifier":"EXACT"},"end":{"value":995,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000023","properties":[{"key":"ProteinId","value":"GAA5130991.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001500804","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:0009338","properties":[{"key":"GoTerm","value":"C:exodeoxyribonuclease V complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008854","properties":[{"key":"GoTerm","value":"F:exodeoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd22352","properties":[{"key":"EntryName","value":"RecB_C-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.320.10","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":"Gene3D","id":"1.10.486.10","properties":[{"key":"EntryName","value":"PCRA, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01485","properties":[{"key":"EntryName","value":"RecB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011604","properties":[{"key":"EntryName","value":"PDDEXK-like_dom_sf"}]},{"database":"InterPro","id":"IPR004586","properties":[{"key":"EntryName","value":"RecB"}]},{"database":"InterPro","id":"IPR011335","properties":[{"key":"EntryName","value":"Restrct_endonuc-II-like"}]},{"database":"InterPro","id":"IPR000212","properties":[{"key":"EntryName","value":"UvrD-like"}]},{"database":"InterPro","id":"IPR014016","properties":[{"key":"EntryName","value":"UvrD-like_ATP-bd"}]},{"database":"InterPro","id":"IPR014017","properties":[{"key":"EntryName","value":"UvrD-like_C"}]},{"database":"PANTHER","id":"PTHR11070:SF23","properties":[{"key":"EntryName","value":"RECBCD ENZYME SUBUNIT RECB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070","properties":[{"key":"EntryName","value":"UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00580","properties":[{"key":"EntryName","value":"UvrD-helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13361","properties":[{"key":"EntryName","value":"UvrD_C"},{"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":"SSF52980","properties":[{"key":"EntryName","value":"Restriction endonuclease-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51198","properties":[{"key":"EntryName","value":"UVRD_HELICASE_ATP_BIND"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51217","properties":[{"key":"EntryName","value":"UVRD_HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLAPAAFDVCGELPTRTTVLEASAGTGKTFTIAALATRYVAEGRASLPELMLVTFGREATQELRERVRERLVTAERGLADPAAARAGADDVLRLLAEAPDAEVAARRARLARAVTQFDAATIATTHQFCQQMLAGLGVAGDGDRDATFVESIEDILAEVVDDFYVRKYGARGAGTPDFSRREALTLARRAVHDGQARLEPRGAEPGTAAHVRYRFATAVRAEVARRKRVRRIYTYDDMLTRLADALADPARGAAARLRARYRVVLVDEFQDTDPVQWQILRKAFHGSTALVLIGDPKQAIYAFRGADVVSYLDATEAADHHATLARNWRSDAVLLEALDTVFAGAALGDPRITVHPVESAHPGSRLRGAPVDTPFRLRVASRAGLPKAPRRDLAVVAPARELVTRDAASDIAALLASPASVDGEPVAPGHVAVLVRTNDQGAMIRQALAAAGVPAVLSGTASVFGTPVAGEWLTLLEALEQPRAARVRAAALTPFLGHTVAELCGPHAESLLDEVGATLRAWAAVLHERGVAALLEAITTRTGLPGRLLGVADGERLLTDLRHIAQTLHAAAASEHLGPAALVEWLRHRIADAAQDVVVERSRRLESDADAVQIITIHRSKGLEFPIVYVPFAWDRNVRDPDVPLLHDESGARVLDVGGESGEGWKERVARHRAEEAGEDLRLLYVALTRARCQVVTWWVPATTTATSPLHRLLIGRPDAGRDPAEAYRVPADNAALHALRELAGSRISVEEIGFSRAALTFSAPAPAADELRAAEFSRHLDIAWRRTSYSALTADAAHGHGPGVGSEPEAPEIDDEAAVELAATSDLPGADLPSPMAELPLGAGFGTLVHGIFEAADLTAADLAGELTARAREQLVHHPVPGVEAERLAAALLPAARTPLGPLAGGLRLADIAPRDRLAELDFELPLAGGDEPGPPVTLGALAPLLRRHLPADDPLRNYPDALAALAEQPLRGYLTGSIDAVLRLPGPRFAVVDYKTNWLGPMGPDGRDPLTSAHYTPPRLAEAMIAAHYPLQALLYGVALHRYLRWRLPGYAPERHLGGVLYLFVRGMCGPDTPAVGGVPCGVFSWAPPAALVQELSGLLDGERA","length":1107,"molWeight":118116,"crc64":"33DC1639127D24FF","md5":"4D902044D955C640919D64AFCE2E3A6F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":4},"uniParcId":"UPI00337A9BAE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NSK9","uniProtkbId":"A0ABP9NSK9_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5129626.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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:0000313","source":"EMBL","id":"GAA5129626.1"}],"value":"katG_3"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"katG"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5129626.1"}],"value":"GCM10023320_50450"}]}],"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":"GAA5129626.1"}],"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":147,"modifier":"EXACT"},"end":{"value":433,"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":43,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"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":277,"modifier":"EXACT"},"end":{"value":277,"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":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-113)","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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000020","properties":[{"key":"ProteinId","value":"GAA5129626.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345607772.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000020.1"}]},{"database":"Proteomes","id":"UP001500804","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":"FunFam","id":"1.10.520.10:FF:000004","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":"MSDSHDATGNNSVLSEVNEESAGGCPISAGRRNHPTEGAGNRDWWPNQLNLKILRKHQPASDPMGADFDYAAEFQTLDLDALARDVDEVLTTSQDWWPADFGHYGPLMIRMAWHSAGTYRIEDGRGGAGAGMQRFAPLNSWPDNVNLDKARRLLWPVKKKYGRKISCADLMIFAGNRALETMGFKTFGFAGGRADVWEPDEDVYWGPERTWLGDERYTGDRELESPLAAVQMGLIYVNPEGPNGNPDPLASARDIRETFRRMAMNDEETVALIAGGHTFGKTHGAAPESHKGPEPEGAPLEEQGLGWKSEFGTGKGRDAIGSGLEVTWTPTPTQWSNWFFHNLFEYDWELTESPAGAKQWTPKDGKARNTVPDPEDGKLNRAPSMLTSDLALRFDPVYEPISRRFYENPDEFADAFARAWYKLTHRDMGPIQRYLGPLVPQETLIWQDPLPAVDHELVDAADIAALKQQILASGLSVAQLVSTAWASASTFRTSDKRGGANGARIRLQPQRGWEVNDPDTLSHVLTTLEGIQESFNSAQTGGKKVSLADLIVLGGVAGVEQAARNAGHEVQVPFTPGRTDATQQQTDVESFAPLEPRADGFRNYRGKGNPLPSEYLLLDRANLLDLTAPEMTVLVGGLRVLGANFQQSPLGVFTSRTESLTNDFFVNLLDMDTTWKPASEDAETFEGRDRATGEVKWTASRVDLVFGSNSELRALAEVYGSDDAQEKFVRDFAAAFAKVMDLDRYDVA","length":748,"molWeight":82487,"crc64":"E8AAAB52B35415EF","md5":"B9740E89CF0DB1F550599D513C464AFA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI0031E91185"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9NTV3","uniProtkbId":"A0ABP9NTV3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128628.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5128628.1"}],"value":"GCM10023320_47870"}]}],"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":"GAA5128628.1"}],"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":81,"modifier":"EXACT"},"end":{"value":81,"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":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"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":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"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":49,"modifier":"EXACT"},"end":{"value":51,"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":110,"modifier":"EXACT"},"end":{"value":110,"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":139,"modifier":"EXACT"},"end":{"value":140,"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":"UP001500804"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000019","properties":[{"key":"ProteinId","value":"GAA5128628.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_425570642.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000019.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MVPVIGVLALQGDVREHVAALEACGDVRAVPVRRSSELDAVDALVIPGGESTTMSRLLQTFELLDPLRKRIVDGMPAYGSCAGMILLASEVLDGRPDQQQLGGLDVVVRRNAFGRQVDSFETDLEFAGLPDGPVRAVFIRAPWVESVGPAVEVLAAVPPRTLSGADAGPAAGRAVAVRQGAVIATAFHPELTGDLRVHGLFCDLVKRARN","length":210,"molWeight":22165,"crc64":"7B5EFDAF4F4D1B84","md5":"9EB26FFC067F13C2B5389727F2B3546F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI003372F27B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9P217","uniProtkbId":"A0ABP9P217_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5137233.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5137233.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5137233.1"}],"value":"GCM10023320_69590"}]}],"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":"GAA5137233.1"}],"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":112,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":360,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"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":130,"modifier":"EXACT"},"end":{"value":130,"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":133,"modifier":"EXACT"},"end":{"value":133,"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":180,"modifier":"EXACT"},"end":{"value":181,"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":214,"modifier":"EXACT"},"end":{"value":214,"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":237,"modifier":"EXACT"},"end":{"value":239,"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":317,"modifier":"EXACT"},"end":{"value":317,"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":"UP001500804"}],"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":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000036","properties":[{"key":"ProteinId","value":"GAA5137233.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345611102.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000036.1"}]},{"database":"Proteomes","id":"UP001500804","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":"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":"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":"MTALPLVFEAPRRAQPPRHLADLDPADRRAAVGELGLPGFRADQLARHYFGRLTADVDAMTDLPAPARDTLRGLLPPLVTPVLEQACDDGATRKTLWKGHDGTRAESVLMGYPDRATVCVSSQAGCGMACPFCATGQGGLQRNLSTGEIVEQVRQAAAAARDGALGTPMRLSNVVFMGMGEPLANYKRVVAAVRRITSPAPDGLGISARGVTVSTVGLVPAIDRLAAEGLPVTLAVSLHTPDDELRDTLVPVNNRWKVAEVLDAARRYAQTTGRRVSIEYALIRDVNDHGWRADLLGKLLRRHVGPSRVHVNLIPLNPTPGSEWDASPRRVQDEFVARVQAAGVACTVRDTRGREIAAACGQLAAQG","length":367,"molWeight":39223,"crc64":"47A86197B22E137A","md5":"4499D803C4704F451A3C64284D9CB36C"},"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":"UPI0031EDA71F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9P2W9","uniProtkbId":"A0ABP9P2W9_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5138670.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"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":"GAA5138670.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5138670.1"}],"value":"GCM10023320_73400"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO: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":"GAA5138670.1"}],"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":20,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":478,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":26,"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":37,"modifier":"EXACT"},"end":{"value":37,"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":94,"modifier":"EXACT"},"end":{"value":94,"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":99,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":125,"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":125,"modifier":"EXACT"},"end":{"value":125,"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":162,"modifier":"EXACT"},"end":{"value":162,"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":177,"modifier":"EXACT"},"end":{"value":177,"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":192,"modifier":"EXACT"},"end":{"value":192,"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":250,"modifier":"EXACT"},"end":{"value":250,"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":250,"modifier":"EXACT"},"end":{"value":250,"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":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"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":399,"modifier":"EXACT"},"end":{"value":399,"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":402,"modifier":"EXACT"},"end":{"value":402,"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":408,"modifier":"EXACT"},"end":{"value":409,"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":427,"modifier":"EXACT"},"end":{"value":427,"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":445,"modifier":"EXACT"},"end":{"value":445,"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":"UP001500804"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000041","properties":[{"key":"ProteinId","value":"GAA5138670.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345611709.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000041.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"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":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLDPHGRGSSDATPSRPAAAIVLAAGEGTRMRSAVPKVLHPIAGRSLLGHAVHAVAALEPEHLVVVVGAAAEQVREAITGMEGELARPVLAAEQRERRGTGHAVRCALDALPNEVTGPVVVTYGDVPLLEPATIAALVAHHSETGVPLTLLTSDVDDPAGYGRVLRESDGTVTRIVEEADATPEQRAIREINSGVYAFDAAFLLSAIDRLRDTNSQGELYLTDLVKIAHDDGVDVHGVRCRDAWQVQGVNDRVQLATLRAELNRRLLERWMRAGVTVVDPATTWVDVQVRLEPDVVLHPGTQLHGATSVAGGAEIGPDTTLTDCAVGAGAVVVRTHGGDAEIGPGASVGPFAYLRPGARLGERGKIGTFVEVKNSDIGPGTKVPHLTYVGDATIGEHSNIGASSVFVNYDGVRKQRTVVGSHVKTGSDNTFVAPVQIGDGAYTGAGTVVREDIPPGALAVSAGSQRTIEGWVARKRPGTPAAEAAARAADPAIDVHGGTAR","length":501,"molWeight":52180,"crc64":"9673F950D1A2C963","md5":"E6DEAE94BF32EEC1C8DB3F28CF4250C4"},"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":19},"uniParcId":"UPI0031EEB286"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9P4L6","uniProtkbId":"A0ABP9P4L6_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5140756.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"Chaperonin GroEL"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"5.6.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"60 kDa chaperonin"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"Chaperonin-60"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"Cpn60"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5140756.1"}],"value":"groL_2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"groEL"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"groL"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5140756.1"}],"value":"GCM10023320_78810"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000419"}],"value":"Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide.","ecNumber":"5.6.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000419"}],"value":"Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004241"}],"value":"Cell surface","id":"SL-0310"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025702"}],"value":"Secreted, capsule","id":"SL-0033"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004191"}],"value":"Secreted, cell wall","id":"SL-0041"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006607"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000418"}],"value":"Belongs to the chaperonin (HSP60) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5140756.1"}],"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":516,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":476,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00600"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000049","properties":[{"key":"ProteinId","value":"GAA5140756.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345612704.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000049.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0042603","properties":[{"key":"GoTerm","value":"C:capsule"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009986","properties":[{"key":"GoTerm","value":"C:cell surface"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"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:0140662","properties":[{"key":"GoTerm","value":"F:ATP-dependent protein folding chaperone"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042026","properties":[{"key":"GoTerm","value":"P:protein refolding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009408","properties":[{"key":"GoTerm","value":"P:response to heat"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd03344","properties":[{"key":"EntryName","value":"GroEL"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.7.10:FF:000001","properties":[{"key":"EntryName","value":"60 kDa chaperonin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.7.10","properties":[{"key":"EntryName","value":"GroEL"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.560.10","properties":[{"key":"EntryName","value":"GroEL-like equatorial domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.260.10","properties":[{"key":"EntryName","value":"TCP-1-like chaperonin intermediate domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00600","properties":[{"key":"EntryName","value":"CH60"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018370","properties":[{"key":"EntryName","value":"Chaperonin_Cpn60_CS"}]},{"database":"InterPro","id":"IPR001844","properties":[{"key":"EntryName","value":"Cpn60/GroEL"}]},{"database":"InterPro","id":"IPR002423","properties":[{"key":"EntryName","value":"Cpn60/GroEL/TCP-1"}]},{"database":"InterPro","id":"IPR027409","properties":[{"key":"EntryName","value":"GroEL-like_apical_dom_sf"}]},{"database":"InterPro","id":"IPR027413","properties":[{"key":"EntryName","value":"GROEL-like_equatorial_sf"}]},{"database":"InterPro","id":"IPR027410","properties":[{"key":"EntryName","value":"TCP-1-like_intermed_sf"}]},{"database":"NCBIfam","id":"NF000592","properties":[{"key":"EntryName","value":"groEL"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009487","properties":[{"key":"EntryName","value":"groEL"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009488","properties":[{"key":"EntryName","value":"groEL"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009489","properties":[{"key":"EntryName","value":"groEL"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02348","properties":[{"key":"EntryName","value":"GroEL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45633","properties":[{"key":"EntryName","value":"60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00118","properties":[{"key":"EntryName","value":"Cpn60_TCP1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00298","properties":[{"key":"EntryName","value":"CHAPERONIN60"}]},{"database":"SUPFAM","id":"SSF52029","properties":[{"key":"EntryName","value":"GroEL apical domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48592","properties":[{"key":"EntryName","value":"GroEL equatorial domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54849","properties":[{"key":"EntryName","value":"GroEL-intermediate domain like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00296","properties":[{"key":"EntryName","value":"CHAPERONINS_CPN60"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKQISFDETARRALERGVNQLADAVKVTLGPRGRHVVLDKKFGGPTVTNDGVTIAREIDLEDPFENLGAQLAKTVATKTNDVAGDGTTTATVLAQAMVAAGLRNVAAGANPTALGKGISLAAEKVAEVLKEKAIPVEGKAIAQVGTIASREEEIGALISEALSKVGTDGVITVEEGSTLATELEITEGLQFDKGYLSPYFVTDAESMEAVLEDAYVLLHQEKIGAIADLLPLLEKVLGEGKPLLIVAEDVEGEALSTLVVNSIRKTVKVAAVKSPFFGDRRKAFMDDLAIATGGTVIKPEVGLKLAEAGLDLLGRVRRVVVTKDTTTLVEGAGAKDAIDGRIAQLKREIEETDSDWDREKLQERLAKLSGGVAVIKAGAATETALKERKHRIEDAVSATRAAVEEGIVPGGGSALVQAAKSLEGGLDLTGDEATGVAIVQRALSAPLFWIAANGGQEGAVVVGRVAQQEWGQGFNAATVTYGDLLADGVIDPVKVTRSAVVNAASIARMVLTTESSVVDKPEPPAPAAGGHGHGHGHGH","length":540,"molWeight":56094,"crc64":"0F0287B5C71EFE91","md5":"BC7EE61A15CEBFBF35A5499D3E39064B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Region":1,"Coiled coil":1,"Binding site":5},"uniParcId":"UPI0031F17F26"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9P4S3","uniProtkbId":"A0ABP9P4S3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5140805.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5140805.1"}],"value":"GCM10023320_78910"}]}],"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":"GAA5140805.1"}],"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":211,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":218,"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":61,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"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":127,"modifier":"EXACT"},"end":{"value":133,"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":156,"modifier":"EXACT"},"end":{"value":156,"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":159,"modifier":"EXACT"},"end":{"value":159,"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":253,"modifier":"EXACT"},"end":{"value":253,"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":306,"modifier":"EXACT"},"end":{"value":306,"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":357,"modifier":"EXACT"},"end":{"value":357,"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":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000049","properties":[{"key":"ProteinId","value":"GAA5140805.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345612723.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000049.1"}]},{"database":"Proteomes","id":"UP001500804","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":"MRGVWTARQVRDAEAVLLARTPEGALMRRAAFGLAVHARRMLAENGRVAGRRVVLLVGAGNNGGDALWAGMELRRRGVGVTAVLLDPARAHPEGLAALLRAGGRVVDAEAGLVAVAGADLVVDGVVGISGRGALREPAARLVAAVEHAGVPVLAVDLPSGVDPDTGAVDGPAVTAAATVTFGALKPVHVLAAARCGPVHLVDIGLTPLLPEPHARVLDAPDVARRWPVPGPGDDKYTQGVAGIAAGSATYPGAAVLASGAAALATSGMVRFAGSAAPGVRDHWPEVVASGSIEEAGRVQAWAVGPGIGTDDAGRAVLAAAIAAEVPLCVDADAVTLLAAHKDLRDALRGRPVVLTPHDREFARVAGDVGTDRIGAARRAAADLGVTVLLKGNATVVADPDGRALVHPATSSWAATAGSGDVLTGMIGALLAAGLEPWWAAGCAAHVHGLAADLAARGAPAPASRLQAALPAAIRSVRASRR","length":481,"molWeight":48177,"crc64":"50C2B29EA478A6CF","md5":"01DD9C12863F1EA79739633BE5854114"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI0031EF0C2C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N4N8","uniProtkbId":"A0ABP9N4N8_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5109701.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Endonuclease V"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"3.1.21.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Deoxyinosine 3'endonuclease"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Deoxyribonuclease V"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"DNase V"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"nfi"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5109701.1"}],"value":"GCM10023320_00510"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.","ecNumber":"3.1.21.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"value":"Belongs to the endonuclease V family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5109701.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Interaction with target DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00801"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000001","properties":[{"key":"ProteinId","value":"GAA5109701.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043737","properties":[{"key":"GoTerm","value":"F:deoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016891","properties":[{"key":"GoTerm","value":"F:RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003727","properties":[{"key":"GoTerm","value":"F:single-stranded RNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06559","properties":[{"key":"EntryName","value":"Endonuclease_V"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.2170.10","properties":[{"key":"EntryName","value":"archaeoglobus fulgidus dsm 4304 superfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00801","properties":[{"key":"EntryName","value":"Endonuclease_5"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR007581","properties":[{"key":"EntryName","value":"Endonuclease-V"}]},{"database":"PANTHER","id":"PTHR28511","properties":[{"key":"EntryName","value":"ENDONUCLEASE V"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR28511:SF1","properties":[{"key":"EntryName","value":"ENDONUCLEASE V"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04493","properties":[{"key":"EntryName","value":"Endonuclease_5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MHVHLHDLGPTPATLDDAAAQQERLRPLVDTTAPGPTDLRTAAGIDVAHHDGTDEVVAAVVVLDATTLRPVETRTVRGRAGHPYVPGFLALRELPVVTAALEELEHTPDLIVCDGAGVAHPRRFGLACHVGLLTGVPTIGVAKSPPLPFEMPKPARGSWTPQVEGDEVVGRALRTQHGVQPVFVSVGHRIGLDAACEHVLRLARHRLPETTRRADRLARDAALRV","length":225,"molWeight":24077,"crc64":"2C7E171CCF1FA81B","md5":"4636BD56F380D8F0164AB73094C647B8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":2,"Site":1},"uniParcId":"UPI00338A9A44"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N5Q9","uniProtkbId":"A0ABP9N5Q9_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110256.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Glycerol kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"2.7.1.30"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"ATP:glycerol 3-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Glycerokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"GK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110256.1"}],"value":"glpK_2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"glpK"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110256.1"}],"value":"GCM10023320_01810"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054633"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycerol + ATP = sn-glycerol 3-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21644"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17754"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57597"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.30","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052101"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Inhibited by fructose 1,6-bisphosphate (FBP)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005190"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"value":"Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009156"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003733"}],"value":"Belongs to the FGGY kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110256.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Carbohydrate kinase FGGY N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00370"}]},{"type":"Domain","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"Carbohydrate kinase FGGY C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02782"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17754"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"glycerol","id":"ChEBI:CHEBI:17754"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}},{"type":"Binding site","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022798"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0319","category":"Biological process","name":"Glycerol metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00186"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000001","properties":[{"key":"ProteinId","value":"GAA5110256.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345602540.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000001.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004370","properties":[{"key":"GoTerm","value":"F:glycerol kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019563","properties":[{"key":"GoTerm","value":"P:glycerol catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006072","properties":[{"key":"GoTerm","value":"P:glycerol-3-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07769","properties":[{"key":"EntryName","value":"ASKHA_NBD_FGGY_GK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000007","properties":[{"key":"EntryName","value":"Glycerol kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000008","properties":[{"key":"EntryName","value":"Glycerol kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00186","properties":[{"key":"EntryName","value":"Glycerol_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR000577","properties":[{"key":"EntryName","value":"Carb_kinase_FGGY"}]},{"database":"InterPro","id":"IPR018483","properties":[{"key":"EntryName","value":"Carb_kinase_FGGY_CS"}]},{"database":"InterPro","id":"IPR018485","properties":[{"key":"EntryName","value":"FGGY_C"}]},{"database":"InterPro","id":"IPR018484","properties":[{"key":"EntryName","value":"FGGY_N"}]},{"database":"InterPro","id":"IPR005999","properties":[{"key":"EntryName","value":"Glycerol_kin"}]},{"database":"NCBIfam","id":"NF000756","properties":[{"key":"EntryName","value":"glpK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01311","properties":[{"key":"EntryName","value":"glycerol_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10196:SF69","properties":[{"key":"EntryName","value":"GLYCEROL KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10196","properties":[{"key":"EntryName","value":"SUGAR KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02782","properties":[{"key":"EntryName","value":"FGGY_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00370","properties":[{"key":"EntryName","value":"FGGY_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000538","properties":[{"key":"EntryName","value":"GlpK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00933","properties":[{"key":"EntryName","value":"FGGY_KINASES_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00445","properties":[{"key":"EntryName","value":"FGGY_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAEFVGAIDQGTTSTRFMIFDHSGNVKGIHQLEHEQILPEAGWVEHNPVEIWERTTAVVQTALNKTGLGASDLAALGITNQRETAVVWDRNTGRPLYNAIVWQDTRTDRIASALDRDGRGDVIRRKAGLPPATYFSGGKIQWILENVDGAREAAERGDAIFGNTDTWLLWNLTGGRDGGVHVTDPTNASRTMLMNLETLDWDDELLGFFGIPRSMLPEIQPSSHPRGYGTTRANGPLSGEILLTGDLGDQQAATVGQVCFAPGEAKNTYGTGNFMLLNTGTELVRSESGLLTTVCYKFGDEPAVYALEGSIAVTGSAVQWLRDQLGIISGAAQSESLARQVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLSRYNTNAHLARATLEAICYQSRDVADAMEKDSGVHLEVLKVDGGVTANELCMQIQADVLGVPVSRPVVAETTALGAAYAAGLAVGFWKTTEELRSNWNESRRWEPQWSDEQRTTGYERWKKAVTRTLDWVDVD","length":505,"molWeight":55071,"crc64":"4F95887BD79C130E","md5":"7BF42B32BDBAD5F2A3F98C2F54570170"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":23},"uniParcId":"UPI0031E869A3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N5T0","uniProtkbId":"A0ABP9N5T0_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110118.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Glucose-6-phosphate 1-dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"G6PD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"1.1.1.49"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110118.1"}],"value":"zwf_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"zwf"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110118.1"}],"value":"GCM10023320_01500"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15841"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57955"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:61548"}],"ecNumber":"1.1.1.49","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004937"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Belongs to the glucose-6-phosphate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5110118.1"}],"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":172,"modifier":"EXACT"}},"description":"Glucose-6-phosphate dehydrogenase NAD-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00479"}]},{"type":"Domain","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Glucose-6-phosphate dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02781"}]},{"type":"Active site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022526"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0313","category":"Biological process","name":"Glucose metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000001","properties":[{"key":"ProteinId","value":"GAA5110118.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345602505.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000001.1"}]},{"database":"Proteomes","id":"UP001500804","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:0004345","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006006","properties":[{"key":"GoTerm","value":"P:glucose metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009051","properties":[{"key":"GoTerm","value":"P:pentose-phosphate shunt, oxidative branch"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00966","properties":[{"key":"EntryName","value":"G6PD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001282","properties":[{"key":"EntryName","value":"G6P_DH"}]},{"database":"InterPro","id":"IPR022675","properties":[{"key":"EntryName","value":"G6P_DH_C"}]},{"database":"InterPro","id":"IPR022674","properties":[{"key":"EntryName","value":"G6P_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00871","properties":[{"key":"EntryName","value":"zwf"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23429:SF0","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23429","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02781","properties":[{"key":"EntryName","value":"G6PD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00479","properties":[{"key":"EntryName","value":"G6PD_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000110","properties":[{"key":"EntryName","value":"G6PD"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00079","properties":[{"key":"EntryName","value":"G6PDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAADRVDALVIFGATGDLAKLETFPALVGLVDRGVLDVPVIGVAKSGWDLGRFREYAAQSLRDNRIDPESAPARTMLGLLRYVDGDLGDNATYEAMAREMGEGRRALFYLEVPPFLFGRIAEGISKAGRAEGARVMVEKPFGTDLASAIALNETMHRYFPEEAIYRVDHWLGLDPLNDVVVARFANSMIEPLLNRDHVEMIQITMAEAFDVADRGRFYDATGAIRDVVQNHMLQVLATVVANPPDSSGPDSWLDAKSRVISALRPLTPENTVRGQYDGYREVDGVDPLSTVESYVAIRLGLDSWRWAGVPILIRAGKTMPVTATEISIRFKPVPLDVFGVDTTHLANALRFRIWPGTQISLTLAGKKPGAGIEPQLQDLVFAEDSGSDMRPYDRLIGAALDGRRVLFARQDTVEAAWRVVDPVLGDVVPVQQYARGTWGPKEADALLPNGLGWHDPA","length":457,"molWeight":50089,"crc64":"7B16567CF61FA1E8","md5":"4F7FD849701404DF2ACC4A4C56818F07"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":7},"uniParcId":"UPI0031EED340"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N723","uniProtkbId":"A0ABP9N723_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111089.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00069372"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"Glycerol-3-phosphate dehydrogenase [NAD(P)+]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066687"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"1.1.1.94"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00080511"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"NAD(P)H-dependent dihydroxyacetone-phosphate reductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"gpsA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111089.1"}],"value":"GCM10023320_03580"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sn-glycerol 3-phosphate + NAD(+) = dihydroxyacetone phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11092"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57597"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.94","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sn-glycerol 3-phosphate + NADP(+) = dihydroxyacetone phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11096"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57597"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.94","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052716"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:11098"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052716"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"Membrane lipid metabolism; glycerophospholipid metabolism"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011009"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000437"}],"value":"Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111089.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01210"}]},{"type":"Domain","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07479"}]},{"type":"Active site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000114-1"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000114-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000114-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000114-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000114-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000114-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57597"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"sn-glycerol 3-phosphate","id":"ChEBI:CHEBI:57597"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00394"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000001","properties":[{"key":"ProteinId","value":"GAA5111089.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001500804","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:0047952","properties":[{"key":"GoTerm","value":"F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046167","properties":[{"key":"GoTerm","value":"P:glycerol-3-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046168","properties":[{"key":"GoTerm","value":"P:glycerol-3-phosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006650","properties":[{"key":"GoTerm","value":"P:glycerophospholipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.1040.10:FF:000001","properties":[{"key":"EntryName","value":"Glycerol-3-phosphate dehydrogenase [NAD(P)+]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000019","properties":[{"key":"EntryName","value":"Glycerol-3-phosphate dehydrogenase [NAD(P)+]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1040.10","properties":[{"key":"EntryName","value":"N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00394","properties":[{"key":"EntryName","value":"NAD_Glyc3P_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR013328","properties":[{"key":"EntryName","value":"6PGD_dom2"}]},{"database":"InterPro","id":"IPR006168","properties":[{"key":"EntryName","value":"G3P_DH_NAD-dep"}]},{"database":"InterPro","id":"IPR006109","properties":[{"key":"EntryName","value":"G3P_DH_NAD-dep_C"}]},{"database":"InterPro","id":"IPR011128","properties":[{"key":"EntryName","value":"G3P_DH_NAD-dep_N"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF000940","properties":[{"key":"EntryName","value":"PRK00094.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF000942","properties":[{"key":"EntryName","value":"PRK00094.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11728","properties":[{"key":"EntryName","value":"GLYCEROL-3-PHOSPHATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11728:SF1","properties":[{"key":"EntryName","value":"GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07479","properties":[{"key":"EntryName","value":"NAD_Gly3P_dh_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01210","properties":[{"key":"EntryName","value":"NAD_Gly3P_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000114","properties":[{"key":"EntryName","value":"Glycerol-3-P_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00077","properties":[{"key":"EntryName","value":"GPDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVRRVAVLGAGSWGTTFAKVMADAGRDVRLWARRPEVAAAVNERHANPDYLPGVALPALLTATADPAEALDGADAVVFAVPSQTLRANLASWRDLLPPGRTLVSLAKGVELGTLLRMSEVIAEVAGVPAEQVAVVSGPNLAREIAAEEPTATVIACADHDRAVALQQACTTGYFRSYTNTDVIGCELGGAGKNVIALACGIAAGMGLGDNTRASLITRGLAETARLGTALGADPLTFAGLAGLGDLVATCSSPLSRNRTFGEHLGRGESLAQAEAANHGQVAEGVKSCKSICALGDRLGVELPIADAVRRVCHEGLSAAEMGKELISRAPRPE","length":334,"molWeight":34330,"crc64":"9E6060A35FBDF77A","md5":"67F6D65919F455564EE05261A19B3755"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":22},"uniParcId":"UPI0031ED837B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N781","uniProtkbId":"A0ABP9N781_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"GMPMT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"2.4.99.16"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"glgE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111199.1"}],"value":"GCM10023320_03740"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl](n) = [(1->4)-alpha-D-glucosyl](n+2) + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42692"},{"database":"Rhea","id":"RHEA-COMP:9584"},{"database":"Rhea","id":"RHEA-COMP:10183"},{"database":"ChEBI","id":"CHEBI:15444"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:63576"}],"ecNumber":"2.4.99.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048735"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"value":"Belongs to the glycosyl hydrolase 13 family. GlgE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111199.1"}],"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":202,"modifier":"EXACT"},"end":{"value":543,"modifier":"EXACT"}},"description":"Glycosyl hydrolase family 13 catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00642"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}]},{"type":"Active site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}]},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:63576"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"ligand":{"name":"alpha-maltose 1-phosphate","id":"ChEBI:CHEBI:63576"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:63576"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"ligand":{"name":"alpha-maltose 1-phosphate","id":"ChEBI:CHEBI:63576"}},{"type":"Binding site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:63576"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"ligand":{"name":"alpha-maltose 1-phosphate","id":"ChEBI:CHEBI:63576"}},{"type":"Binding site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:63576"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"ligand":{"name":"alpha-maltose 1-phosphate","id":"ChEBI:CHEBI:63576"}},{"type":"Binding site","location":{"start":{"value":527,"modifier":"EXACT"},"end":{"value":528,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:63576"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"ligand":{"name":"alpha-maltose 1-phosphate","id":"ChEBI:CHEBI:63576"}},{"type":"Site","location":{"start":{"value":473,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02124"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"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_02124"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000002","properties":[{"key":"ProteinId","value":"GAA5111199.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004553","properties":[{"key":"GoTerm","value":"F:hydrolase activity, hydrolyzing O-glycosyl compounds"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030979","properties":[{"key":"GoTerm","value":"P:alpha-glucan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd11344","properties":[{"key":"EntryName","value":"AmyAc_GlgE_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1180","properties":[{"key":"EntryName","value":"Golgi alpha-mannosidase II"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.80","properties":[{"key":"EntryName","value":"Phosphotransferase system, lactose/cellobiose-type IIA subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02124","properties":[{"key":"EntryName","value":"GlgE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006047","properties":[{"key":"EntryName","value":"GH13_cat_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR026585","properties":[{"key":"EntryName","value":"GlgE"}]},{"database":"InterPro","id":"IPR049171","properties":[{"key":"EntryName","value":"GLGE_C"}]},{"database":"InterPro","id":"IPR021828","properties":[{"key":"EntryName","value":"GlgE_dom_N/S"}]},{"database":"InterPro","id":"IPR013780","properties":[{"key":"EntryName","value":"Glyco_hydro_b"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"PANTHER","id":"PTHR47786","properties":[{"key":"EntryName","value":"ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47786:SF2","properties":[{"key":"EntryName","value":"GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21702","properties":[{"key":"EntryName","value":"GLGE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11896","properties":[{"key":"EntryName","value":"GlgE_dom_N_S"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00642","properties":[{"key":"EntryName","value":"Aamy"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPMTGRLGIDDVTPTVSGGRHPSKAVVGEVVPITATVWREGHDAVAANVVWRRIGSQGAAHHVRMTPVGSGTDRFAATVVPDEPGLWSFRVDAWSDPWSTWRHAVTVKLSAGQGADELANDLEVGARLLQRVGRRPGERPHRDLLFGAANALRDTALPLHARVAPALFPAVEKIMTERPVRELITRGRAQQIHVDRERALFGSWYEFFPRSTGGVDEQGRPIHGTFVTASKELDRVAAMGFDVVYLPPIHPIGTVHRKGRNNNVNAGPGDVGSPWAIGSADGGHDAIEPELGTIEDFDAFVDRTRDLGMEVALDFALQCAPDHPWVTEHPEWFTVRPDGSIAYAENPPKKYQDIYPVNFDNDPAGIYAESLRVVLHWAEHGVRIFRVDNPHTKPPNFWHWLIWQVKSRYPDVLFLAEAFTRPARLFGLARLGFTQSYTYFTWRTTKAELTDFALMHAERADECRPNFFVNTPDILHESLQTGGPAMFAIRATLASTLSPTWGVYSGFELFESEPVRPGSEEYLNSEKYELRPRDFTAAVNRGRSLEPYLARLNEIRRAHPALQQLRDLHFHEVDNDAIIAYSKTDPATGDTVLVVCTLDSFHPQEGTTALDMPALRAGWNDRLTVHDEITDETYDWGQYNYVRLEPSRNVAHIFRVER","length":658,"molWeight":73814,"crc64":"C8AF8CAC531E8046","md5":"800F434C8A6AA2B375512945EEA1026C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Active site":2,"Binding site":5,"Site":1},"uniParcId":"UPI00337C7F93"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N7R3","uniProtkbId":"A0ABP9N7R3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018679"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00260"}],"value":"Threonine synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013028"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00260"}],"value":"4.2.3.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111511.1"}],"value":"thrC_1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111511.1"}],"value":"GCM10023320_04480"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003648"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"value":"Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O-phospho-L-homoserine + H2O = L-threonine + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10840"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57590"},{"database":"ChEBI","id":"CHEBI:57926"}],"ecNumber":"4.2.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049144"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR038945-1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004979"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"value":"Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005517"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"value":"Belongs to the threonine synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111511.1"}],"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":30,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Tryptophan synthase beta chain-like PALP","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00291"}]},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR038945-1"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR038945-1"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR038945-1"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Modified residue","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR038945-2"}]},{"type":"Cross-link","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR038945-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022697"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038945"}],"id":"KW-0791","category":"Biological process","name":"Threonine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000002","properties":[{"key":"ProteinId","value":"GAA5111511.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_345602871.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABJO010000002.1"}]},{"database":"Proteomes","id":"UP001500804","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003941","properties":[{"key":"GoTerm","value":"F:L-serine ammonia-lyase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004794","properties":[{"key":"GoTerm","value":"F:threonine deaminase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004795","properties":[{"key":"GoTerm","value":"F:threonine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006565","properties":[{"key":"GoTerm","value":"P:L-serine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009088","properties":[{"key":"GoTerm","value":"P:L-threonine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006567","properties":[{"key":"GoTerm","value":"P:L-threonine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01563","properties":[{"key":"EntryName","value":"Thr-synth_1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1100:FF:000014","properties":[{"key":"EntryName","value":"Threonine synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR050147","properties":[{"key":"EntryName","value":"Ser/Thr_Dehydratase"}]},{"database":"InterPro","id":"IPR000634","properties":[{"key":"EntryName","value":"Ser/Thr_deHydtase_PyrdxlP-BS"}]},{"database":"InterPro","id":"IPR004450","properties":[{"key":"EntryName","value":"Thr_synthase-like"}]},{"database":"InterPro","id":"IPR026260","properties":[{"key":"EntryName","value":"Thr_Synthase_bac/arc"}]},{"database":"InterPro","id":"IPR001926","properties":[{"key":"EntryName","value":"TrpB-like_PALP"}]},{"database":"InterPro","id":"IPR036052","properties":[{"key":"EntryName","value":"TrpB-like_PALP_sf"}]},{"database":"NCBIfam","id":"TIGR00260","properties":[{"key":"EntryName","value":"thrC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48078:SF6","properties":[{"key":"EntryName","value":"L-THREONINE DEHYDRATASE CATABOLIC TDCB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48078","properties":[{"key":"EntryName","value":"THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00291","properties":[{"key":"EntryName","value":"PALP"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF038945","properties":[{"key":"EntryName","value":"Thr_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53686","properties":[{"key":"EntryName","value":"Tryptophan synthase beta subunit-like PLP-dependent enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00165","properties":[{"key":"EntryName","value":"DEHYDRATASE_SER_THR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAAQKLTRWPGVIEAYRERMPVQEGWTVVTLGEGGTPLLPAPHLSAATGCEVLLKVDGANPTGSFKDRGMTMAVTHALAEGKQGVLCASTGNTSASAAAYATRAGMTCAVLVPRGKIALGKLAQAVAHGARILQIDGNFDDCLELARKTTADYPVAALVNSVNPTRIAGQASAAYEICDELGRAPDVHCLPVGNAGNITAYWQGYRAYLADGLIHTPPRMFGFQAAGAAPLVRGEPVVAPETIATAIRIGAPASWAGAMKARDESDGRFAAVTDDEILSAYRLLSAREGVFVEPASAASVAGLLQSAADGTLPRGSLVVCTVTGHGLKDPDTALLAAPEPTVVPIDPGAVAAALELR","length":358,"molWeight":36815,"crc64":"ADE0EB99EE13CBA9","md5":"745287A712A5CE9C5E5B61BF13A3E6EE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3,"Modified residue":1,"Cross-link":1},"uniParcId":"UPI0031EC0378"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABP9N7S7","uniProtkbId":"A0ABP9N7S7_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudonocardia adelaidensis","taxonId":648754,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111505.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Pseudonocardia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097693"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Transcription termination factor Rho"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00767"}],"value":"3.6.4.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"ATP-dependent helicase Rho"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"rho"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111505.1"}],"value":"GCM10023320_04460"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Facilitates transcription termination from RNA polymerase (RNAP) by binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, translocation in a 5'-3' direction on the RNA (toward RNAP), and release of the RNA from the DNA template"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Plays a major role in reduction of R-loop formation across the genome; R-loops can be generated by annealing of untranslated, (often antisense) RNA to upstream DNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049360"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Homohexamer. The homohexamer assembles into a catalytically inactive open ring structure; the active homohexamer is a closed ring which encircles RNA. Contacts RNA polymerase (RNAP) via its C-terminal domains, allowing RNA to pass through the central channel"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"value":"The N-terminus consists of a helical bundle and an OB-fold which form the primary RNA-binding site (PBS, part of Rho RNA-BD) on the surface of the hexameric ring. The N-terminus is joined by a linker to the C-terminal domain, which has a RecA-type fold. Six C-terminal domains form a central channel through which single-stranded (ss)RNA passes; ATP binds between the protomers. The secondary RNA-binding site (SBS) is formed by Q- and R-loops in the center of the ring which recognize pyrimidine-rich RNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01203"}],"value":"Belongs to the Rho family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GAA5111505.1"}],"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":364,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"Rho RNA-BD","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51856"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":593,"modifier":"EXACT"},"end":{"value":604,"modifier":"EXACT"}},"description":"Q-loop","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}]},{"type":"Motif","location":{"start":{"value":636,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"R-loop","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}]},{"type":"Compositional bias","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":483,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":499,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":526,"modifier":"EXACT"},"end":{"value":526,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":680,"modifier":"EXACT"},"end":{"value":680,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":681,"modifier":"EXACT"},"end":{"value":681,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022472"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01884"}],"id":"KW-0806","category":"Biological process","name":"Transcription termination"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}],"value":"JCM 18302","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001500804"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BAABJO010000002","properties":[{"key":"ProteinId","value":"GAA5111505.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001500804","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:0008186","properties":[{"key":"GoTerm","value":"F:ATP-dependent activity, acting on RNA"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004386","properties":[{"key":"GoTerm","value":"F:helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006353","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription termination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01128","properties":[{"key":"EntryName","value":"rho_factor_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01884","properties":[{"key":"EntryName","value":"Rho"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR011129","properties":[{"key":"EntryName","value":"CSD"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011112","properties":[{"key":"EntryName","value":"Rho-like_N"}]},{"database":"InterPro","id":"IPR041703","properties":[{"key":"EntryName","value":"Rho_factor_ATP-bd"}]},{"database":"InterPro","id":"IPR036269","properties":[{"key":"EntryName","value":"Rho_N_sf"}]},{"database":"InterPro","id":"IPR011113","properties":[{"key":"EntryName","value":"Rho_RNA-bd"}]},{"database":"InterPro","id":"IPR004665","properties":[{"key":"EntryName","value":"Term_rho"}]},{"database":"NCBIfam","id":"NF006886","properties":[{"key":"EntryName","value":"rho"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00767","properties":[{"key":"EntryName","value":"rho"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46425","properties":[{"key":"EntryName","value":"TRANSCRIPTION TERMINATION FACTOR RHO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46425:SF1","properties":[{"key":"EntryName","value":"TRANSCRIPTION TERMINATION FACTOR RHO"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07498","properties":[{"key":"EntryName","value":"Rho_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07497","properties":[{"key":"EntryName","value":"Rho_RNA_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00357","properties":[{"key":"EntryName","value":"CSP"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00959","properties":[{"key":"EntryName","value":"Rho_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF68912","properties":[{"key":"EntryName","value":"Rho N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51856","properties":[{"key":"EntryName","value":"RHO_RNA_BD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSETDLVSTEAAPAPRKRGGLSGMVLAELRQLAGELNIPDIAGMRKGDLIAAIKEKQGAPQRRKRSAAAQQTLPGTGEESAAPASAEAPAVNGAAPAAEAAPAAAVAEPAPAAEPTRRRRAASRPAGAPSVASPPATSPPATSEPAASEPATSTVNGAAVADAAPVADAAPAAPAAEPAPEAENGAAPAGEAVEAAAPTRRSRQSRRNRAEQQAEQAQQAAEPTSSAAASSAPATSAPAEERQRDGGRDGGDARPDSRREGGRDRDRGGRDGGRESGRDNNRADNRGDRDNRGDRPDNRADTRSDPRGPRDNRPDDDGDDDGDGRGRRGRRFRDRRRGRDRDRDRTGGGGQGNVDTEVRDGDVLLPVAGIVDILDNYAFVRTTGYLSGPTDVYVSLSMVRKYGLRRGDAITGAVREPREGEQSRQKFNPLVRVDSINGQDPETSKQRPEFTKLTPLYPNERLRLETEPHKLTTRVIDLVMPVGKGQRALIVSPPKAGKTTIMQNIANAITTNNPECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDRPPTDHTTVAELSIERAKRLVELGHDVVVLLDNITRLGRAYNLAAPASGRILSGGVDSTALYPPKRFLGAARNIEDGGSLTIFATALVETGSTMDTVIFEEFKGTGNAELKLDRKIADKRVFPAIDVGDSGTRKEELIMSPDEYAVMVKLRRVLAALDDQQAIDLLLTQLRKTRTNIEFLMQVAKSTPGNDND","length":740,"molWeight":78820,"crc64":"BFDD0A1FE1379C86","md5":"F157726416908062D517CCDACF10802F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Motif":2,"Compositional bias":6,"Binding site":6},"uniParcId":"UPI0031EABA1E"}}]}