{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DXA4","uniProtkbId":"CAP15_YERAE","entryAudit":{"firstPublicDate":"2024-03-27","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-03-27","entryVersion":9,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34784509"}],"value":"CD-NTase-associated protein 15"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34784509"}],"value":"YaCap15"}]}},"genes":[{"geneName":{"value":"cap15"},"orfNames":[{"value":"FS896_RS19155"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34784509"}],"value":"Effector protein of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnE) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The C-terminal beta barrel binds to and is stabilized by cyclic dinucleotides; 3',3'-cyclic UMP-UMP (c-di-UMP), 3',3'-cyclic UMP-AMP (c-di-UAMP), 3',3'-cyclic UMP-GMP (c-di-UGMP) and 3',3'-cyclic UMP-CMP (c-di-UCMP) bind to and stabilize the beta barrel whereas 3',3'-cyclic di-AMP (c-di-AMP) does not bind the beta barrel (PubMed:34784509). Upon binding of c-di-UMP (or another cyclic dinucleotide) probably oligomerizes, inducing cell membrane shrinkage and rupture, leading to cell death (Probable) (PubMed:34784509)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"value":"Protects E.coli against phage infection. When the CBASS operon (cap15-cdnE) is introduced in E.coli MG1655 it protects against phages T2, T4, T5, T6, SECPhi4, SECPhi6, SECPhi17, SECPhi18 and SECPhi27, but not against phage T7 (PubMed:34784509)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34784509"}],"value":"The beta barrel domain oligomerizes; in the presence of c-di-UMP or c-di-UAMP higher-level oligomers are detected (PubMed:34784509)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34784509"}],"value":"In the absence of cyclic dinucleotides forms puncta mostly found at the cell poles. In the presence of cyclic dinucleotides redistributes as puncta over the cell inner membrane as it collapses away from the cell wall; cells die rapidly as the cell inner membrane shrinks from the cell wall"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DXA2"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"value":"Cell toxicity relies on the transmembrane domain; its replacement by a SUMO domain prevents cell death in cells also expressing DncV from V.cholerae (PubMed:34784509). The C-terminus (residues 78-208) forms a minimal, eight-stranded beta barrel (PubMed:34784509). Trp-96 stacks against Arg-204 and forms a hydrogen bond with Leu-92 to close the barrel. A set of conserved residues in the 'top' of the barrel (Thr-129; Tyr-153; Tyr-155; Asn-157; Tyr-188 and Met-200) surround a probable cyclic dinucleotide-binding site; when mutated these residues decrease or abolish nucleotide binding and impact protection against phage in vivo (PubMed:34784509). In the C-terminus two possible oligomerization domains have been identified. In interface 1 beta-strand 1 (residues 78-88) forms an anti-parallel beta-sheet with beta-strand 1 from a neighboring subunit and is further stabilized by inter-subunit stacking of Trp-120. Interface 2 is formed by hydrophobic residues facing out of the barrel (Ile-142; Leu-152; Phe-172; Phe-189 and Tyr-197)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the CBASS Cap15 membrane effector family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"CD-NTase-associated protein 15","featureId":"PRO_0000459803"},{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Mutagenesis","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Beta barrel no longer oligomerizes, dimerizes in presence of 3',3'-cyclic di-UMP (c-di-UMP) or 3',3'-cyclic UMP-AMP (c-di-UAMP); when associated with A-120.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"Complete loss of protection against all phage tested in E.coli, beta barrel no longer oligomerizes, dimerizes in presence of c-di-UMP or c-di-UAMP; when associatd with 78-W--C-88 del.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Beta barrel no longer binds c-di-UMP.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Complete loss of protection against all phage tested in E.coli.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Beta barrel has decreased ability to bind c-di-UMP, no change in protection against phage in E.coli.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Beta barrel has decreased ability to bind c-di-UMP, no change in protection against phage in E.coli.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Beta barrel no longer binds c-di-UMP, complete loss of protection against all phage tested in E.coli.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Complete loss of protection against all phage tested in E.coli.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Beta barrel no longer binds c-di-UMP.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Beta barrel has decreased ability to bind c-di-UMP, decreased protein stability.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"M","alternativeSequences":["I"]}},{"type":"Beta strand","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N35"}]},{"type":"Beta strand","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Turn","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]},{"type":"Beta strand","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7N34"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0051","category":"Biological process","name":"Antiviral defense"},{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3EE7COP1LHN9","citationType":"submission","authors":["Criscuolo A."],"publicationDate":"JUL-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"IP28587","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"CABHQK010000182"}]},{"referenceNumber":2,"citation":{"id":"34784509","citationType":"journal article","authors":["Duncan-Lowey B.","McNamara-Bordewick N.K.","Tal N.","Sorek R.","Kranzusch P.J."],"citationCrossReferences":[{"database":"PubMed","id":"34784509"},{"database":"DOI","id":"10.1016/j.molcel.2021.10.020"}],"title":"Effector-mediated membrane disruption controls cell death in CBASS antiphage defense.","publicationDate":"2021","journal":"Mol. Cell","firstPage":"5039","lastPage":"5051.e5","volume":"81"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","FUNCTION","SUBUNIT","DOMAIN","NUCLEOTIDE-BINDING","MUTAGENESIS OF 78-TRP--CYS-88; TRP-120; THR-129; LEU-152; TYR-153; TYR-155; ASN-157; PHE-172; TYR-188 AND MET-200"],"evidences":[{"evidenceCode":"ECO:0000312","source":"PDB","id":"7N34"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"7N35"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CABHQK010000182","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_145567547.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQK010000182.1"}]},{"database":"PDB","id":"7N34","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=78-208"}]},{"database":"PDB","id":"7N35","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B=78-208"}]},{"database":"AlphaFoldDB","id":"P0DXA4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0DXA4","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"InterPro","id":"IPR041208","properties":[{"key":"EntryName","value":"Cap15"}]},{"database":"InterPro","id":"IPR056338","properties":[{"key":"EntryName","value":"Cap15-like_TM"}]},{"database":"Pfam","id":"PF18153","properties":[{"key":"EntryName","value":"Cap15_CD_rec"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23471","properties":[{"key":"EntryName","value":"Cap15_TM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKSHEYIVICGLNRSKVGRYIAIVASFLSFISIFLALTALEWLKNYHINSHIPASVFSLISAGGIYMGLYAWFDKNLWQNSYLGKFLCVPNLEGRWHVDGHTRSEGGNTWEGELKIVQTWDKVRIHLKTKASHSDSVTASIIYDKGIGYQLLYNYRNQPKTGEEHLTSHVGFAEFRFDADLKSAEGHYFNGQGRATYGTMTITRIEHA","length":208,"molWeight":23641,"crc64":"597489DF84DCC65F","md5":"B0786E95A38646BAA854A7131FC5599D"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":2,"Mutagenesis":10,"Beta strand":9,"Turn":1},"uniParcId":"UPI0011A0899C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DXA5","uniProtkbId":"CDNE_YERAE","entryAudit":{"firstPublicDate":"2024-03-27","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-03-27","entryVersion":8,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"}],"value":"Cyclic dinucleotide synthase CdnE"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34784509"}],"value":"Ya-CdnE02"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"value":"2.7.7.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34784509"}],"value":"cGAS/DncV-like nucleotidyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32839535"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34784509"}],"value":"CD-NTase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34784509"}],"value":"cdnE"},"orfNames":[{"value":"FS896_RS19160"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32839535"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34784509"}],"value":"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:34784509). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15 (PubMed:34784509). A type I-B(UU) CBASS system (PubMed:32839535)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"value":"Cyclic dinucleotide synthase that preferentially catalyzes the synthesis of 3',3'-cyclic UMP-UMP (c-di-UMP) and 3',3'-cyclic UMP-AMP, with minor amounts of 3',3'-cyclic UMP-CMP, which are second messengers for cell signal transduction (PubMed:34784509)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"value":"Protects E.coli against phage infection. When the CBASS operon (cap15-cdnE) is introduced in E.coli MG1655 it protects against phages T2, T4, T5, T6, SECPhi4, SECPhi6, SECPhi17, SECPhi18 and SECPhi27, but not against phage T7 (PubMed:34784509)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 UTP = c-di-UMP + 2 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60480"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:143807"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60481"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + ATP = 3',3'-cUAMP + 2 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60456"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:143809"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60457"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + CTP = cyclic CMP-UMP + 2 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60484"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:143811"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60485"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"value":"Binds 2 Mg(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"value":"The (R/Q)xW motif controls pyrimidine nucleotide specificity in the donor pocket, while conserved Asn-229 is important for recognition of uracil in the acceptor pocket"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the CD-NTase family. E02 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Cyclic dinucleotide synthase CdnE","featureId":"PRO_0000459801"},{"type":"Motif","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Pyrimidine specificity motif (R/Q)xW in donor pocket","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}]},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"acceptor"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"donor"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"acceptor"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"acceptor"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"acceptor"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"donor"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398","label":"donor"}},{"type":"Site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Important for uracil base recognition in acceptor pocket","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DSP3"}]},{"type":"Mutagenesis","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"No longer protects against phage.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34784509"}],"alternativeSequence":{"originalSequence":"DVD","alternativeSequences":["AVA"]}}],"keywords":[{"id":"KW-0051","category":"Biological process","name":"Antiviral defense"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3EE7COP1LHN9","citationType":"submission","authors":["Criscuolo A."],"publicationDate":"JUL-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"IP28587","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"32839535","citationType":"journal article","authors":["Millman A.","Melamed S.","Amitai G.","Sorek R."],"citationCrossReferences":[{"database":"PubMed","id":"32839535"},{"database":"DOI","id":"10.1038/s41564-020-0777-y"}],"title":"Diversity and classification of cyclic-oligonucleotide-based anti-phage signalling systems.","publicationDate":"2020","journal":"Nat. Microbiol.","firstPage":"1608","lastPage":"1615","volume":"5"},"referencePositions":["CLASSIFICATION AND NOMENCLATURE"]},{"referenceNumber":3,"citation":{"id":"34784509","citationType":"journal article","authors":["Duncan-Lowey B.","McNamara-Bordewick N.K.","Tal N.","Sorek R.","Kranzusch P.J."],"citationCrossReferences":[{"database":"PubMed","id":"34784509"},{"database":"DOI","id":"10.1016/j.molcel.2021.10.020"}],"title":"Effector-mediated membrane disruption controls cell death in CBASS antiphage defense.","publicationDate":"2021","journal":"Mol. Cell","firstPage":"5039","lastPage":"5051.e5","volume":"81"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","DOMAIN","MUTAGENESIS OF 121-ASP--ASP-123"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CABHQK010000182","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_145567548.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQK010000182.1"}]},{"database":"AlphaFoldDB","id":"P0DXA5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0DXA5","properties":[{"key":"Description","value":"-"}]},{"database":"InterPro","id":"IPR058909","properties":[{"key":"EntryName","value":"CD_NTase_C"}]},{"database":"Pfam","id":"PF26305","properties":[{"key":"EntryName","value":"CD_NTase_C"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPNPAFSARIERMKLRRKGTSDQLRVATESISNQRYDGLEKYTLLEDVLHLSESWENRGKGDSAIRYIIGAMQPVDARYTEISFETASRIENQLSKKLAHNLDFRVQGSVPLDIHIKGFSDVDLLIIDTQMLMYDVNGGGSYSPTSRDGRDVIIELREAARDALEMAFPTALVDDNNAKSLRITGGSLQREVDVVPSIWWDTKEYQSMKREEDRGVTIIDKNTRERIYNAPFLHIKRIKDKCDQCNGGIRKSIRLLKTLKADSKDEGSDIDLSSYDIASLMFHADANNLNHSTYYELAVLVETHRLLNYLSQNYEVAMQLDVPNGTRKIFEKPESHVELLKLTEMVNSVVTEVLREITGRPTDFYANDKCDVLRKQMVY","length":379,"molWeight":43322,"crc64":"7E560866BBD1CF9C","md5":"E251EF300E6DF0DB20C360A61008C990"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Motif":1,"Binding site":10,"Site":1,"Mutagenesis":1},"uniParcId":"UPI0011AAB70D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9TK33","uniProtkbId":"A0A0T9TK33_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":34,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34580.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00071120"}],"value":"Acyl-CoA thioesterase 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038894"}],"value":"3.1.2.20"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00079653"}],"value":"Thioesterase II"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34580.1"}],"value":"ACZ76_14085"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055321"}],"value":"Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA. Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)-octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively. Seems to be involved in 3-hydroxyalkanoate production in E.coli"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-dodecenoyl-CoA + H2O = (2E)-dodecenoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65212"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57330"},{"database":"ChEBI","id":"CHEBI:84274"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050629"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65213"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050629"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3E,5Z)-tetradecadienoyl-CoA + H2O = (3E,5Z)-tetradecadienoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:55044"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:71586"},{"database":"ChEBI","id":"CHEBI:71590"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050558"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:55045"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050558"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3R)-3-hydroxybutanoyl-CoA + H2O = (R)-3-hydroxybutanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65204"},{"database":"ChEBI","id":"CHEBI:10983"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051737"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65205"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051737"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3R)-3-hydroxypentanoyl-CoA + H2O = (3R)-3-hydroxypentanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:55084"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:138587"},{"database":"ChEBI","id":"CHEBI:138588"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051978"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:55085"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051978"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3S)-3-hydroxybutanoyl-CoA + H2O = (S)-3-hydroxybutanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65208"},{"database":"ChEBI","id":"CHEBI:11047"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57316"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052191"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65209"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052191"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3S)-3-hydroxypentanoyl-CoA + H2O = (3S)-3-hydroxypentanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:55096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:138607"},{"database":"ChEBI","id":"CHEBI:138608"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050803"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:55097"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050803"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3Z,5E)-dodecadienoyl-CoA + H2O = (3Z,5E)-dodecadienoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65172"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:156333"},{"database":"ChEBI","id":"CHEBI:156334"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050889"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65173"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050889"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40139"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30823"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57387"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40140"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-hydroxydodecanoyl-CoA + H2O = 3-hydroxydodecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65232"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:76616"},{"database":"ChEBI","id":"CHEBI:156383"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050660"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65233"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050660"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-oxododecanoyl-CoA + H2O = 3-oxododecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65216"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29743"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:62615"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051093"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65217"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051093"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-methylpentanoyl-CoA + H2O = 4-methylpentanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:55064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:74904"},{"database":"ChEBI","id":"CHEBI:131445"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050380"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:55065"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050380"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16781"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:77636"}],"ecNumber":"3.1.2.20","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050943"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:16782"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050943"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + H2O = butanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40111"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17968"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57371"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000295"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40112"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000295"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"decanoyl-CoA + H2O = decanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40059"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:27689"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:61430"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047969"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40060"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047969"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dodecanoyl-CoA + H2O = dodecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30135"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:18262"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57375"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048074"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30136"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048074"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexadecanoyl-CoA + H2O = hexadecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16645"},{"database":"ChEBI","id":"CHEBI:7896"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57379"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052691"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:16646"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052691"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + H2O = hexanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40115"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17120"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050199"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40116"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050199"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octadecanoyl-CoA + H2O = octadecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30139"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:25629"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051478"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30140"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051478"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octanoyl-CoA + H2O = octanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30143"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:25646"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57386"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047588"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30144"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047588"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pentanoyl-CoA + H2O = pentanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:55052"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:31011"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57389"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050810"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:55053"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050810"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tetradecanoyl-CoA + H2O = tetradecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40119"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30807"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57385"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048180"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40120"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048180"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006538"}],"value":"Belongs to the C/M/P thioester hydrolase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"Acyl-CoA thioesterase-like N-terminal HotDog","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13622"}]},{"type":"Domain","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"Acyl-CoA thioesterase 2 C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02551"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34580.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34580.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34580.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619483.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQI010000023.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9TK33","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61902718","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_14085","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9781019at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0047617","properties":[{"key":"GoTerm","value":"F:fatty acyl-CoA hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006637","properties":[{"key":"GoTerm","value":"P:acyl-CoA metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009062","properties":[{"key":"GoTerm","value":"P:fatty acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03444","properties":[{"key":"EntryName","value":"Thioesterase_II_repeat1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03445","properties":[{"key":"EntryName","value":"Thioesterase_II_repeat2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.160.210:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA thioesterase II"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.160.210","properties":[{"key":"EntryName","value":"Acyl-CoA thioesterase, double hotdog domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR042171","properties":[{"key":"EntryName","value":"Acyl-CoA_hotdog"}]},{"database":"InterPro","id":"IPR003703","properties":[{"key":"EntryName","value":"Acyl_CoA_thio"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"InterPro","id":"IPR049449","properties":[{"key":"EntryName","value":"TesB_ACOT8-like_N"}]},{"database":"InterPro","id":"IPR025652","properties":[{"key":"EntryName","value":"TesB_C"}]},{"database":"NCBIfam","id":"NF007817","properties":[{"key":"EntryName","value":"tesB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00189","properties":[{"key":"EntryName","value":"tesB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11066","properties":[{"key":"EntryName","value":"ACYL-COA THIOESTERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11066:SF34","properties":[{"key":"EntryName","value":"ACYL-COENZYME A THIOESTERASE 8"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13622","properties":[{"key":"EntryName","value":"4HBT_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02551","properties":[{"key":"EntryName","value":"Acyl_CoA_thio"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSQPLAKLLDLLHLEKIEEGIFRGQSEDLGLRQVFGGQVVGQAIYAAKQTVPIDRIVHSFHSYFLRPGDSSKPIIYDVETLRDGTSFSARRISAIQNGKPIFYMTASFQSQEEGFEHQNTMPEVPSPDGLMSETDIARKFAHLIPEKVREKFIGNQPIEMRPVKFHNPLQGSVEEPNRYVWFRANGEIPDDLRVHQYLLGYASDFNFLPTALQPHGIGFLEPGVQIATIDHSMWFHRPFRLDDWLLYAVESTSASGARGFVRGQIYNQQGVLVASTVQEGVIRLHR","length":286,"molWeight":32407,"crc64":"BB6B42D628701C9E","md5":"7831EFF81645D0BD257F756B9D50CF53"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":21,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI0005E49C92"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UDM7","uniProtkbId":"A0ABM5UDM7_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Fatty acid oxidation complex subunit alpha"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"4.2.1.17"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"5.1.2.3"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"5.3.3.8"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"3-hydroxyacyl-CoA dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"1.1.1.35"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33957.1"}],"value":"fadB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33957.1"}],"value":"ACZ76_10570"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21760"},{"database":"ChEBI","id":"CHEBI:57315"},{"database":"ChEBI","id":"CHEBI:57316"}],"ecNumber":"5.1.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45228"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:85097"}],"ecNumber":"5.3.3.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22432"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:90726"}],"ecNumber":"1.1.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049556"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16105"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:58856"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45900"},{"database":"ChEBI","id":"CHEBI:85097"},{"database":"ChEBI","id":"CHEBI:85489"}],"ecNumber":"5.3.3.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20724"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:137480"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005005"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00065953"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Heterotetramer of two alpha chains (FadB) and two beta chains (FadA)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008750"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007005"}],"value":"In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00378"}]},{"type":"Domain","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase NAD binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02737"}]},{"type":"Domain","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":592,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Domain","location":{"start":{"value":627,"modifier":"EXACT"},"end":{"value":684,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Region","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":729,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Active site","location":{"start":{"value":450,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"For 3-hydroxyacyl-CoA dehydrogenase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":500,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":660,"modifier":"EXACT"},"end":{"value":660,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022963"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"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_01621"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33957.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618911.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000013.1"}]},{"database":"GeneID","id":"61903393","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_10570","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0036125","properties":[{"key":"GoTerm","value":"C:fatty acid beta-oxidation multienzyme complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008692","properties":[{"key":"GoTerm","value":"F:3-hydroxybutyryl-CoA epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004165","properties":[{"key":"GoTerm","value":"F:delta(3)-delta(2)-enoyl-CoA isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004300","properties":[{"key":"GoTerm","value":"F:enoyl-CoA hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016509","properties":[{"key":"GoTerm","value":"F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070403","properties":[{"key":"GoTerm","value":"F:NAD+ binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006635","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1040.50:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid oxidation complex subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000018","properties":[{"key":"EntryName","value":"Fatty acid oxidation complex subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000009","properties":[{"key":"EntryName","value":"Fatty oxidation complex, alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1040.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01621","properties":[{"key":"EntryName","value":"FadB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006180","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR006176","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR006108","properties":[{"key":"EntryName","value":"3HC_DH_C"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR018376","properties":[{"key":"EntryName","value":"Enoyl-CoA_hyd/isom_CS"}]},{"database":"InterPro","id":"IPR001753","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra/iso"}]},{"database":"InterPro","id":"IPR050136","properties":[{"key":"EntryName","value":"FA_oxidation_alpha_subunit"}]},{"database":"InterPro","id":"IPR012799","properties":[{"key":"EntryName","value":"FadB"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF008727","properties":[{"key":"EntryName","value":"fadB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02437","properties":[{"key":"EntryName","value":"FadB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612:SF3","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00725","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02737","properties":[{"key":"EntryName","value":"3HCDH_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00067","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00166","properties":[{"key":"EntryName","value":"ENOYL_COA_HYDRATASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLYQSETLQLHWLENGIAELVFDAPGSVNKLDTKTVANLGEALAVLEKQSELKGLLLRSAKAAFIVGADITEFLSLFNAPPEKLHQWLVFANDIFNRLEDLPVPTISAINGYALGGGCECILATDFRVASPETRIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDIVAKDALKVGLVDAVVTAEKLTEAALVMLKQAIDGKLDWQAARRPKLEPLKLNPTEAAMCFTIAKGMVMQVAGKHYPAPLTAVKTIEAAAKFGRTEALKLETNSFVPLAGSNEARALVGIFLNDQYVKGQAKKLSKGVNAPKQAAVLGAGIMGGGIAYQSALKGVPVIMKDINDKSLTIGMNEAAKLLNKQLERGKIDGLKMANILATIQPTLDYTGIERAQLIVEAVVENPRIKAAVLAETEALISEDAVLASNTSTIPIDQLAKSLQRPENFCGMHFFNPVHRMPLVEIIRGAKTSDKTIAAVVAYATQMGKTPIVVNDCPGFFVNRVLFPYLAGFGMLVRDGGDFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAVGFPDRMNKDYRDAVDVMFDNQRFGQKNGQGFYRYTQDAKGKPRKENDEQVDTLLAAISQPTQKFSDDNIIARTMIPMINEVVRCLEEGIIASPAEGDIALVYGLGFPPFHGGIFRYLDTIGSANYVEMAQRYTHLGALYHVPAGLRAKAEHNESYYPVAAALLDVSTSQPA","length":729,"molWeight":78850,"crc64":"E0F8CDE94A7A6002","md5":"CA9C4FE66EE523FD0F46A3B8262A25C3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":3},"countByFeatureType":{"Domain":4,"Region":2,"Active site":1,"Binding site":9,"Site":2},"uniParcId":"UPI0005E9DB86"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UFS5","uniProtkbId":"A0ABM5UFS5_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074468"}],"value":"Thioesterase 1/protease 1/lysophospholipase L1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013277"}],"value":"3.1.1.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013274"}],"value":"3.1.1.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012480"}],"value":"3.1.2.14"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038848"}],"value":"3.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00080218"}],"value":"Acyl-CoA thioesterase 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00080229"}],"value":"Acyl-CoA thioesterase I"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00079606"}],"value":"Arylesterase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076150"}],"value":"Lysophospholipase L1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00082145"}],"value":"Oleoyl-[acyl-carrier-protein] hydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00079125"}],"value":"Phospholipid degradation C"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078270"}],"value":"Protease 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078278"}],"value":"Protease I"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078117"}],"value":"Thioesterase I/protease I"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34628.1"}],"value":"ACZ76_14360"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(11Z)-octadecenoyl-CoA + H2O = (11Z)-octadecenoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65240"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30827"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:75121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052958"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65241"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052958"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40151"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:32395"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57368"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00035852"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40152"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00035852"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40131"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:32372"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:61540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050352"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:40132"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050352"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15057"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9924"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30823"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78783"}],"ecNumber":"3.1.2.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052435"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:15058"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052435"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1-acyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + a fatty acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15177"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16870"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:58168"}],"ecNumber":"3.1.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049531"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47348"},{"database":"ChEBI","id":"CHEBI:2571"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17968"},{"database":"ChEBI","id":"CHEBI:50477"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050473"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16781"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:77636"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052976"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:16782"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052976"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a hexanoate ester + H2O = an aliphatic alcohol + hexanoate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47352"},{"database":"ChEBI","id":"CHEBI:2571"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17120"},{"database":"ChEBI","id":"CHEBI:87656"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052918"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a phenyl acetate + H2O = a phenol + acetate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:33853"},{"database":"ChEBI","id":"CHEBI:140310"}],"ecNumber":"3.1.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000368"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an octanoate ester + H2O = an aliphatic alcohol + octanoate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47356"},{"database":"ChEBI","id":"CHEBI:2571"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:25646"},{"database":"ChEBI","id":"CHEBI:87657"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052268"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexadecanoyl-CoA + H2O = hexadecanoate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16645"},{"database":"ChEBI","id":"CHEBI:7896"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57379"}],"ecNumber":"3.1.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047734"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:16646"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047734"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00065151"}],"value":"Monomer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008668"}],"value":"Belongs to the 'GDSL' lipolytic enzyme family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Thioesterase 1/protease 1/lysophospholipase L1","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5045389784"},{"type":"Domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"SGNH hydrolase-type esterase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13472"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34628.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619534.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000008.1"}]},{"database":"GeneID","id":"61902771","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_14360","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0004064","properties":[{"key":"GoTerm","value":"F:arylesterase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004622","properties":[{"key":"GoTerm","value":"F:phosphatidylcholine lysophospholipase A1 activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006629","properties":[{"key":"GoTerm","value":"P:lipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01822","properties":[{"key":"EntryName","value":"Lysophospholipase_L1_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1110:FF:000001","properties":[{"key":"EntryName","value":"Multifunctional acyl-CoA thioesterase I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1110","properties":[{"key":"EntryName","value":"SGNH hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051532","properties":[{"key":"EntryName","value":"Ester_Hydrolysis_Enzymes"}]},{"database":"InterPro","id":"IPR008265","properties":[{"key":"EntryName","value":"Lipase_GDSL_AS"}]},{"database":"InterPro","id":"IPR013830","properties":[{"key":"EntryName","value":"SGNH_hydro"}]},{"database":"InterPro","id":"IPR036514","properties":[{"key":"EntryName","value":"SGNH_hydro_sf"}]},{"database":"NCBIfam","id":"NF007819","properties":[{"key":"EntryName","value":"tesA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30383","properties":[{"key":"EntryName","value":"THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30383:SF24","properties":[{"key":"EntryName","value":"THIOESTERASE 1_PROTEASE 1_LYSOPHOSPHOLIPASE L1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13472","properties":[{"key":"EntryName","value":"Lipase_GDSL_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52266","properties":[{"key":"EntryName","value":"SGNH hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01098","properties":[{"key":"EntryName","value":"LIPASE_GDSL_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFKNVFRWHLPFLLLLGLFSLRAAATDTLLILGDSLSAGYRLPIAEAWPTRLDKTWQVTPALPKVVNASISGDTAAQGLARLPALLKQHQPRWVLIELGANDGLRGFPTQDIQRDLTQIINLVKEVNAQPLLMQIRIPPNYGRRYTDAFTAMYPQLAQQFDIPLVPFFMEHVAVKPEWMQDDGLHPNAEAQPFIADWMAQQLKPLVTNKQ","length":211,"molWeight":23860,"crc64":"F71ABA840A6CBEC1","md5":"58B1F648E3C69F1C37218278410C8B0E"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":11,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1},"uniParcId":"UPI00065DBD50"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9SZ70","uniProtkbId":"A0A0T9SZ70_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":46,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34289.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072883"},{"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":"ARBA","id":"ARBA00066633"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075482"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076158"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081560"},{"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34289.1"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34289.1"}],"value":"ACZ76_12445"}]}],"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":"ARBA","id":"ARBA00050251"},{"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"}],"features":[{"type":"Domain","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"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":29,"modifier":"EXACT"},"end":{"value":29,"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":44,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":122,"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":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":159,"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":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"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":390,"modifier":"EXACT"},"end":{"value":390,"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":414,"modifier":"EXACT"},"end":{"value":417,"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":465,"modifier":"EXACT"},"end":{"value":465,"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":469,"modifier":"EXACT"},"end":{"value":469,"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":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"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":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"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":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34289.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34289.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34289.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619204.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000420.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9SZ70","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61901063","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_12445","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"FunFam","id":"3.40.1190.10:FF:000006","properties":[{"key":"EntryName","value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.190.20:FF:000006","properties":[{"key":"EntryName","value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"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":"NF001123","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"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":"MADRNLRDLLAPWGLDVPERALREMTLDSRVAAAGDLFVAIVGHQTDGRRYIPQAIAQGVAAIVAEADGVAPDASVAEMHGVPVIYLRNLNQHLSTLAGQFYHQPGAALRLVGVTGTNGKTTTTQLLAQWSQALGETSAVMGTVGNGLLGQVIPTENTTGSAVDIQHLLRNLVDQGATFAAMEVSSHGLIQNRVAALPFAAAVFTNLSRDHLDYHGNMASYEAAKWLLFSTHQSEHKIINADDEVGRRWLSQLPQAVAVSMEGHVPAGWKGPWLSASHVEYHDNGASIAFNSSWGEGQIESRLMGAFNVSNLLVALSTLLSLGYPLDQLLAAAPHLQPVCGRMEVFNAPGKPTVVVDYAHTPDALEKALAAARLHCKGQLWCVFGCGGDRDKGKRPLMGGIAEQLADRVVVTDDNPRSEEPQAIVADILSGLLDAGHALAIHGRAEAVTSAIMQAKEDDVVLIAGKGHEDYQLVGNRRLDYSDRVTVARLLGVVA","length":495,"molWeight":52806,"crc64":"88E2DC114036E77F","md5":"5AA66F75192B64485F4E94D7305A1B5A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":13,"Modified residue":1},"uniParcId":"UPI0005E3FFD7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9T0Q3","uniProtkbId":"A0A0T9T0Q3_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":46,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34253.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"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":"AKP34253.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34253.1"}],"value":"ACZ76_12255"}]}],"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"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1077,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5048419632"},{"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":937,"modifier":"EXACT"},"end":{"value":1077,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":553,"modifier":"EXACT"}},"description":"Oligomerization domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":554,"modifier":"EXACT"},"end":{"value":936,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":937,"modifier":"EXACT"},"end":{"value":1077,"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"}},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34253.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34253.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34253.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619176.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9T0Q3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61901101","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_12255","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804197at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000004","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHNMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCAIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFSVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTLQESMQKALRGLEVGATGFDPKVSLDDPEALTKIRRELKEAGSDRIWYIADAFRAGMSVDGVFNLTNVDRWFLVQIEELVRLEENVAECGINGLNAEFMRQLKRKGFADARLAKLVGAAESEVRKLRYKHGLHPVYKRVDTCAAEFSTDTAYMYSTYEEECESNPTSDRPKVMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFESVTLEDVLEIVRIEKPQGVIVQYGGQTPLKLARELEAAGVPVIGTSPDAIDRAEDRERFQQAVNRLGLKQPANATVATIEQAVEKATGLGYPLVVRPSYVLGGRAMEIVYDEVDLRRYFQNAVSVSNDAPVLLDRFLDDAVEVDVDAICDGERVLIGGIMEHIEQAGVHSGDSACSLPAYTLSKEIQDVMRQQVEKLAFELCVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGMPLAKIAARVMVGQSLAEQGITEEIIPPYYSVKEVVLPFNKFPGVDPILGPEMRSTGEVMGVGRTFAEAFSKAMLGSQSGMKKSGRALLSVREGDKHRVVDLAAKLLKQGFELDATHGTAVVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIVNTTAGRQAIEDSKLIRRSALQYKVHYDTTLNGGFATAMALNADPTEQVISVQEMHAKIKNMKG","length":1077,"molWeight":118154,"crc64":"B66C0C7D28512862","md5":"0EFF7755C2FF9D8774BF6F3793A6924A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":3,"Region":4,"Binding site":38,"Lipidation":2},"uniParcId":"UPI0005E68DCC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9T456","uniProtkbId":"A0A0T9T456_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":39,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34019.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"5-keto-4-deoxy-D-glucarate aldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"KDGluc aldolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"KDGlucA"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"4.1.2.20"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"2-dehydro-3-deoxy-D-glucarate aldolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"2-keto-3-deoxy-D-glucarate aldolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"5-dehydro-4-deoxy-D-glucarate aldolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Alpha-keto-beta-deoxy-D-glucarate aldolase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"garL"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34019.1"}],"value":"ACZ76_10950"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-dehydro-3-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate + pyruvate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10268"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:57978"},{"database":"ChEBI","id":"CHEBI:58098"}],"ecNumber":"4.1.2.20","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-dehydro-4-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate + pyruvate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27726"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:42819"},{"database":"ChEBI","id":"CHEBI:57978"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glyceraldehyde + pyruvate = 2-dehydro-3-deoxy-L-galactonate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:80055"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:17378"},{"database":"ChEBI","id":"CHEBI:75545"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045074"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Carbohydrate acid metabolism; galactarate degradation; D-glycerate from galactarate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Homohexamer; trimer of dimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"HpcH/HpaI aldolase/citrate lyase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03328"}]},{"type":"Active site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}]},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}]},{"type":"Site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"Increases basicity of active site His","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01291"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34019.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34019.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34019.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618969.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHPU010000063.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9T456","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61901357","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_10950","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"86160at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0008672","properties":[{"key":"GoTerm","value":"F:2-dehydro-3-deoxyglucarate aldolase 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:0046392","properties":[{"key":"GoTerm","value":"P:D-galactarate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042838","properties":[{"key":"GoTerm","value":"P:D-glucarate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.20.20.60:FF:000004","properties":[{"key":"EntryName","value":"5-keto-4-deoxy-D-glucarate aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.60","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate-binding domains"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01291","properties":[{"key":"EntryName","value":"KDGluc_aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005000","properties":[{"key":"EntryName","value":"Aldolase/citrate-lyase_domain"}]},{"database":"InterPro","id":"IPR017648","properties":[{"key":"EntryName","value":"GarL"}]},{"database":"InterPro","id":"IPR050251","properties":[{"key":"EntryName","value":"HpcH-HpaI_aldolase"}]},{"database":"InterPro","id":"IPR015813","properties":[{"key":"EntryName","value":"Pyrv/PenolPyrv_kinase-like_dom"}]},{"database":"InterPro","id":"IPR040442","properties":[{"key":"EntryName","value":"Pyrv_kinase-like_dom_sf"}]},{"database":"NCBIfam","id":"NF007849","properties":[{"key":"EntryName","value":"garL"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR03239","properties":[{"key":"EntryName","value":"GarL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30502","properties":[{"key":"EntryName","value":"2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30502:SF4","properties":[{"key":"EntryName","value":"5-KETO-4-DEOXY-D-GLUCARATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03328","properties":[{"key":"EntryName","value":"HpcH_HpaI"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51621","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate/pyruvate domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSLQNYPNQFRRSLKEGQTLIGCWSALANHISAEVLGLAGFDWLVLDGEHAPNDVTTFIPQLMALKGSHSAPVVRAPCNEPIIIKRLLDIGFYNFLIPFVESEEEAIRAVASTRYPPAGIRGVSVSHRGNNYGTVPDYFATINDNITVLVQIESQLGVDNLDAIAAVEGVDGIFVGPGDLSAALGYLGQPNHPEVQKVIRHIFDRAKAQGKPSGILAPVDADARRYLEWGATFVAVGSDLGIFRSATQALCDKFKK","length":256,"molWeight":27729,"crc64":"DB9B4AF4B5741FE1","md5":"11F801E8D3CF062B8C6C8B347D92A7FF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":4,"Site":2},"uniParcId":"UPI0005DCDA6A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9T4U9","uniProtkbId":"A0A0T9T4U9_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":57,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34047.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"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":"AKP34047.1"}],"value":"ACZ76_11115"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":75,"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":72,"modifier":"EXACT"},"end":{"value":72,"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":135,"modifier":"EXACT"},"end":{"value":135,"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":139,"modifier":"EXACT"},"end":{"value":145,"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":150,"modifier":"EXACT"},"end":{"value":150,"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":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"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":269,"modifier":"EXACT"},"end":{"value":269,"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":329,"modifier":"EXACT"},"end":{"value":329,"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":375,"modifier":"EXACT"},"end":{"value":375,"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":412,"modifier":"EXACT"},"end":{"value":416,"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":441,"modifier":"EXACT"},"end":{"value":441,"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":442,"modifier":"EXACT"},"end":{"value":442,"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:0000313","source":"EMBL","id":"AKP34047.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_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":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34047.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34047.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34047.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34047.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618992.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9T4U9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61901324","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_11115","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9806925at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"3.40.1190.20:FF:000017","properties":[{"key":"EntryName","value":"Multifunctional fusion protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10260:FF:000003","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":"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":"NF007856","properties":[{"key":"EntryName","value":"nnr"},{"key":"MatchStatus","value":"1"}]},{"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":"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":"MTDHSKKQIGVSLPHSVFSADWVRQNEAIAAAHFSLNLFDLMVRAGDAAFELARKQYPTARHWLILCGHGNNGGDGYIVANRALAAGLNVTLIACPGNRPLPAEAHQAQSQWLAAGGVINPPDIPWPSHVDLIIDGLLGIGLRAAPQGVYATLIDTANRHRAAKIALDIPSGLSADSGAAPGSVIRADHTLTFVALKPGLLTGQARDWVGHLHCNDLGLTQWLAAQPVQIERMTAEHLPQWLRPRRPCAHKGEHGRLLLVGGDKGLGGAIRMAGEAALRSGAGLVRVLTHIEHVAPILAARPELMVQELTDETLEQSIRWADVLVVGPGLGQSDWGRNALNLLQQSDKPALWDADALNLLALNPLKRQNRVLTPHPGEAARLLGCRVADIESDRLLSARNIVKQYGGVVVLKGAGTLIASEQGEMAIADVGNAGMASGGMGDILSGIIGSLIAQKLVLYDAACAGCVVHGVAADKLAEVQGTRGLLATDLLPVIPKYVNPELAR","length":504,"molWeight":53293,"crc64":"4492FB8DD0EE1EB7","md5":"402791FA586F6A112B1CCE0BE6DA0C6B"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4},"countByFeatureType":{"Domain":2,"Binding site":13},"uniParcId":"UPI0005DFC244"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9TIR9","uniProtkbId":"A0A0T9TIR9_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":37,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34522.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Pyrimidine/purine nucleoside phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Adenosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Cytidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Guanosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Inosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Thymidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Uridine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Xanthosine phosphorylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"ppnP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34522.1"}],"value":"ACZ76_13775"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19805"},{"database":"ChEBI","id":"CHEBI:26386"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"},{"database":"ChEBI","id":"CHEBI:142355"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27642"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine + phosphate = cytosine + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:52540"},{"database":"ChEBI","id":"CHEBI:16040"},{"database":"ChEBI","id":"CHEBI:17562"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13233"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:16750"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27646"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"thymidine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + thymine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16037"},{"database":"ChEBI","id":"CHEBI:17748"},{"database":"ChEBI","id":"CHEBI:17821"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57259"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine + phosphate = alpha-D-ribose 1-phosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24388"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"xanthosine + phosphate = alpha-D-ribose 1-phosphate + xanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27638"},{"database":"ChEBI","id":"CHEBI:17712"},{"database":"ChEBI","id":"CHEBI:18107"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Belongs to the nucleoside phosphorylase PpnP family"}],"commentType":"SIMILARITY"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34522.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34522.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34522.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_004873495.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHPU010000116.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9TIR9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61817576","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61902656","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_13775","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793848at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004731","properties":[{"key":"GoTerm","value":"F:purine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016154","properties":[{"key":"GoTerm","value":"F:pyrimidine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"2.60.120.10:FF:000016","properties":[{"key":"EntryName","value":"Pyrimidine/purine nucleoside phosphorylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01537","properties":[{"key":"EntryName","value":"Nucleos_phosphorylase_PpnP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009664","properties":[{"key":"EntryName","value":"Ppnp"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"NCBIfam","id":"NF007875","properties":[{"key":"EntryName","value":"ppnP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36540","properties":[{"key":"EntryName","value":"PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36540:SF1","properties":[{"key":"EntryName","value":"PYRIMIDINE_PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06865","properties":[{"key":"EntryName","value":"Ppnp"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLKFNEYFTGKVKSIGFDSDSIGPASVGVMEKGEYTFSTAKPEEMTVITGSLKVLIPGSSGWEVFKPGETFYIPGESEFNLQVAEASSYLCKYLS","length":95,"molWeight":10381,"crc64":"3642B70CD9812660","md5":"B6460602EA67B56DE1AEBD00C74C405A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"SIMILARITY":1},"uniParcId":"UPI00005F80EC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9TTL6","uniProtkbId":"A0A0T9TTL6_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":62,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34372.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Siroheme synthase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Uroporphyrinogen-III C-methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Urogen III methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"2.1.1.107"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"SUMT"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Uroporphyrinogen III methylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"UROM"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Precorrin-2 dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"1.3.1.76"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Sirohydrochlorin ferrochelatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"4.99.1.4"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"cysG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34372.1"}],"value":"ACZ76_12905"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"precorrin-2 + NAD(+) = sirohydrochlorin + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58351"},{"database":"ChEBI","id":"CHEBI:58827"}],"ecNumber":"1.3.1.76","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047561"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"siroheme + 2 H(+) = sirohydrochlorin + Fe(2+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24360"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:58351"},{"database":"ChEBI","id":"CHEBI:60052"}],"ecNumber":"4.99.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrinogen III + 2 S-adenosyl-L-methionine = precorrin-2 + 2 S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32459"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57308"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:58827"},{"database":"ChEBI","id":"CHEBI:59789"}],"ecNumber":"2.1.1.107","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060548"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025705"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005010"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005879"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003960"}],"value":"Belongs to the precorrin methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"In the C-terminal section; belongs to the precorrin methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Siroheme synthase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14824"}]},{"type":"Domain","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Sirohaem synthase dimerisation","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10414"}]},{"type":"Domain","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"Tetrapyrrole methylase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00590"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]},{"type":"Region","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Uroporphyrinogen-III C-methyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]},{"type":"Active site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR036426-1"}]},{"type":"Active site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR036426-1"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Modified residue","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022573"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0169","category":"Biological process","name":"Cobalamin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"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_01646"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"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_01646"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34372.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34372.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34372.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619273.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQI010000099.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9TTL6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61904121","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_12905","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9815856at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043115","properties":[{"key":"GoTerm","value":"F:precorrin-2 dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004325","properties":[{"key":"GoTerm","value":"F:protoporphyrin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051266","properties":[{"key":"GoTerm","value":"F:sirohydrochlorin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004851","properties":[{"key":"GoTerm","value":"F:uroporphyrin-III C-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009236","properties":[{"key":"GoTerm","value":"P:cobalamin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019354","properties":[{"key":"GoTerm","value":"P:siroheme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd11642","properties":[{"key":"EntryName","value":"SUMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.160.110:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.950.10:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1010.10:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1010.10","properties":[{"key":"EntryName","value":"Cobalt-precorrin-4 Transmethylase, Domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.950.10","properties":[{"key":"EntryName","value":"Methyltransferase, Cobalt-precorrin-4 Transmethylase, 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":"Gene3D","id":"1.10.8.210","properties":[{"key":"EntryName","value":"Sirohaem synthase, dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.160.110","properties":[{"key":"EntryName","value":"Siroheme synthase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01646","properties":[{"key":"EntryName","value":"Siroheme_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000878","properties":[{"key":"EntryName","value":"4pyrrol_Mease"}]},{"database":"InterPro","id":"IPR035996","properties":[{"key":"EntryName","value":"4pyrrol_Methylase_sf"}]},{"database":"InterPro","id":"IPR014777","properties":[{"key":"EntryName","value":"4pyrrole_Mease_sub1"}]},{"database":"InterPro","id":"IPR014776","properties":[{"key":"EntryName","value":"4pyrrole_Mease_sub2"}]},{"database":"InterPro","id":"IPR006366","properties":[{"key":"EntryName","value":"CobA/CysG_C"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR050161","properties":[{"key":"EntryName","value":"Siro_Cobalamin_biosynth"}]},{"database":"InterPro","id":"IPR037115","properties":[{"key":"EntryName","value":"Sirohaem_synt_dimer_dom_sf"}]},{"database":"InterPro","id":"IPR012409","properties":[{"key":"EntryName","value":"Sirohaem_synth"}]},{"database":"InterPro","id":"IPR028281","properties":[{"key":"EntryName","value":"Sirohaem_synthase_central"}]},{"database":"InterPro","id":"IPR019478","properties":[{"key":"EntryName","value":"Sirohaem_synthase_dimer_dom"}]},{"database":"InterPro","id":"IPR006367","properties":[{"key":"EntryName","value":"Sirohaem_synthase_N"}]},{"database":"InterPro","id":"IPR003043","properties":[{"key":"EntryName","value":"Uropor_MeTrfase_CS"}]},{"database":"NCBIfam","id":"TIGR01469","properties":[{"key":"EntryName","value":"cobA_cysG_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF007922","properties":[{"key":"EntryName","value":"cysG"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01470","properties":[{"key":"EntryName","value":"cysG_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004790","properties":[{"key":"EntryName","value":"PRK06136.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45790:SF1","properties":[{"key":"EntryName","value":"SIROHEME SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45790","properties":[{"key":"EntryName","value":"SIROHEME SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10414","properties":[{"key":"EntryName","value":"CysG_dimeriser"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13241","properties":[{"key":"EntryName","value":"NAD_binding_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14824","properties":[{"key":"EntryName","value":"Sirohm_synth_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00590","properties":[{"key":"EntryName","value":"TP_methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF036426","properties":[{"key":"EntryName","value":"Sirohaem_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75615","properties":[{"key":"EntryName","value":"Siroheme synthase middle domains-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53790","properties":[{"key":"EntryName","value":"Tetrapyrrole methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00839","properties":[{"key":"EntryName","value":"SUMT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00840","properties":[{"key":"EntryName","value":"SUMT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDYLPLFADLKQRPVLVVGGGEVAARKIELLHRAGAQVRVVAQTLSSELEQQYLDDRIHWQAKVFLPEQLDEVFLVIAATNDTALNAAVFAAADQRHILANVVDDQPLCSFIFPSIVDRSPLVVAISSAGQAPVLARILREKLEALLPASLGDMAAVAGRWRSRVKQQIHSMGARRRFWENAFSGRFASLISRGQLAQAEDELQQSIAGQGSTLGEVALVGAGPGDPGLLTLRGLQVIQQADVVLYDHLVSPEVLDLVRRDAERICVGKRAGAHSVAQEETNQLLVTLAQQGKRVVRLKGGDPFIFGRGGEELQVVARAGIAFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRSDGGELDWQALARGRQTLAIYMGTVKAAEISQQLITHGRASTTPVAVISRGTRADQQVRTGTLAQLESLAHQAPTPALLVIGEVVDLHHQIAWFGQQQQTEQAISPSVVNLA","length":472,"molWeight":50701,"crc64":"3B2A375D7914AB10","md5":"5DD2FE1708A0B133D57B2323378E6244"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"PATHWAY":5,"SIMILARITY":3},"countByFeatureType":{"Domain":3,"Region":2,"Active site":2,"Binding site":8,"Modified residue":1},"uniParcId":"UPI0005DF1446"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9U4P1","uniProtkbId":"A0A0T9U4P1_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":57,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33174.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Bifunctional protein HldE"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 7-phosphate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"2.7.1.167"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 7-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-glycero-beta-D-manno-heptose-7-phosphate kinase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 1-phosphate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"2.7.7.70"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"hldE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33174.1"}],"value":"ACZ76_06260"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003753"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002319"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27465"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:59967"},{"database":"ChEBI","id":"CHEBI:61593"}],"ecNumber":"2.7.7.70","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glycero-beta-D-manno-heptose 7-phosphate + ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27473"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:60204"},{"database":"ChEBI","id":"CHEBI:60208"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.167","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052873"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004713"}],"value":"Bacterial outer membrane biogenesis; LPS core biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061122"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"In the C-terminal section; belongs to the cytidylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060955"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"In the N-terminal section; belongs to the carbohydrate kinase PfkB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Domain","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Ribokinase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Region","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"Cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Active site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"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_01603"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"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_01603"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33174.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33174.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33174.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048617797.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHPU010000025.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9U4P1","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61903372","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_06260","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802794at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"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:0033785","properties":[{"key":"GoTerm","value":"F:heptose 7-phosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033786","properties":[{"key":"GoTerm","value":"F:heptose-1-phosphate adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016773","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, alcohol group as acceptor"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0097171","properties":[{"key":"GoTerm","value":"P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009244","properties":[{"key":"GoTerm","value":"P:lipopolysaccharide core region biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd01172","properties":[{"key":"EntryName","value":"RfaE_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1190.20:FF:000002","properties":[{"key":"EntryName","value":"Bifunctional protein HldE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000028","properties":[{"key":"EntryName","value":"Bifunctional protein HldE"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01603","properties":[{"key":"EntryName","value":"HldE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023030","properties":[{"key":"EntryName","value":"Bifunc_HldE"}]},{"database":"InterPro","id":"IPR002173","properties":[{"key":"EntryName","value":"Carboh/pur_kinase_PfkB_CS"}]},{"database":"InterPro","id":"IPR004821","properties":[{"key":"EntryName","value":"Cyt_trans-like"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR011913","properties":[{"key":"EntryName","value":"RfaE_dom_I"}]},{"database":"InterPro","id":"IPR011914","properties":[{"key":"EntryName","value":"RfaE_dom_II"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00125","properties":[{"key":"EntryName","value":"cyt_tran_rel"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008454","properties":[{"key":"EntryName","value":"hldE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02198","properties":[{"key":"EntryName","value":"rfaE_dom_I"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02199","properties":[{"key":"EntryName","value":"rfaE_dom_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46969","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN HLDE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46969:SF1","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN HLDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01467","properties":[{"key":"EntryName","value":"CTP_transf_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00583","properties":[{"key":"EntryName","value":"PFKB_KINASES_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKVTLPDFRRAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAISRLVGLTGIDDAARALTSKLNEVQVRCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFDGIDPQPIFERIQQALPQIGALVLSDYAKGALNSVQPMIQLARKAKVPVLIDPKGSDFERYRGATLLTPNLSEFEAVVGHCKNEEELVSRGMKLVADFELSALLVTRSEQGMTLLQLGKPPLHLPTQAQEVFDVTGAGDTVIGVLAAALAAGNTLEESCFLANAAAGVVVGKLGTSTVSPIELENAIRGRAETGFGVMDEQQLKKAVAQARQRGEKVVMTNGIFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGEKRPVNPLDQRMIVLGALEAVDWVVPFEEDTPQRLIADILPDLLVKGGDYKPDEIAGSAEVWAAGGEVKVLNFEDGVSTTNIIQSIKNGRG","length":476,"molWeight":51176,"crc64":"5A115A631F61B01E","md5":"0991D40D833BDD1B5C9ACC588257BF52"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":1},"uniParcId":"UPI0005DC54C5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9U8N2","uniProtkbId":"A0A0T9U8N2_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-02-17","entryVersion":47,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33466.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Acetylornithine/succinyldiaminopimelate aminotransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"ACOAT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"DapATase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Succinyldiaminopimelate transferase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"2.6.1.11"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"2.6.1.17"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33466.1"}],"value":"argD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"dapC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33466.1"}],"value":"ACZ76_07925"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Involved in both the arginine and lysine biosynthetic pathways"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18049"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29123"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57805"}],"ecNumber":"2.6.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-succinyl-(2S,6S)-2,6-diaminopimelate + 2-oxoglutarate = (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11960"},{"database":"ChEBI","id":"CHEBI:15685"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58087"}],"ecNumber":"2.6.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Binds 1 pyridoxal phosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57805"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"ligand":{"name":"N(2)-acetyl-L-ornithine","id":"ChEBI:CHEBI:57805"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57805"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"ligand":{"name":"N(2)-acetyl-L-ornithine","id":"ChEBI:CHEBI:57805"}},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Modified residue","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01107"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"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_01107"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33466.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33466.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33466.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618281.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000005.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9U8N2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61902004","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_07925","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801052at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003992","properties":[{"key":"GoTerm","value":"F:N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009016","properties":[{"key":"GoTerm","value":"F:succinyldiaminopimelate:2-oxoglutarate transaminase activity"},{"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":"CDD","id":"cd00610","properties":[{"key":"EntryName","value":"OAT_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000004","properties":[{"key":"EntryName","value":"Acetylornithine aminotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01107","properties":[{"key":"EntryName","value":"ArgD_aminotrans_3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017652","properties":[{"key":"EntryName","value":"Ac/SucOrn_transaminase_bac"}]},{"database":"InterPro","id":"IPR004636","properties":[{"key":"EntryName","value":"AcOrn/SuccOrn_fam"}]},{"database":"InterPro","id":"IPR005814","properties":[{"key":"EntryName","value":"Aminotrans_3"}]},{"database":"InterPro","id":"IPR049704","properties":[{"key":"EntryName","value":"Aminotrans_3_PPA_site"}]},{"database":"InterPro","id":"IPR050103","properties":[{"key":"EntryName","value":"Class-III_PLP-dep_AT"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR03246","properties":[{"key":"EntryName","value":"arg_catab_astC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00707","properties":[{"key":"EntryName","value":"argD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002325","properties":[{"key":"EntryName","value":"PRK01278.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003468","properties":[{"key":"EntryName","value":"PRK05093.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009047","properties":[{"key":"EntryName","value":"PRK12381.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11986:SF122","properties":[{"key":"EntryName","value":"ACETYLORNITHINE_SUCCINYLDIAMINOPIMELATE AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11986","properties":[{"key":"EntryName","value":"AMINOTRANSFERASE CLASS III"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00202","properties":[{"key":"EntryName","value":"Aminotran_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000521","properties":[{"key":"EntryName","value":"Transaminase_4ab_Lys_Orn"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00600","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADKLAVNRSTFDQVILPVYAPAQFIPVKGKGSRVWDQQGTEYVDFAGGIAVTALGHCHPALVAALHQQGETLWHTSNVFTNEPALRLAQKLIAATFADRVFFANSGGEANEAAFKLARHYAIERHSPYKTKIIAFHNAFHGRTLFTVSVGGQPKYSDGFGPKPADIIHVPFNDLAAVKAVMDDHTCAVVLEPIQGEGGITAATLEFLQGVRDLCTQHKALLVFDEVQSGMGRSGKLFTYMHYGVTPDILTTAKALGGGFPISAMLTTEEIASVMAVGTHGTTYGGNPLACAVAEAALDVINTPEVLEGIEQRHGLFVQALQVINRKYSVFSDIRGMGLLIGAELAPQYRGRAREFLTAAAAQGLMILNAGPDVLRLAPSLVIELDDIQQGMACLERAIASLVNGN","length":406,"molWeight":43437,"crc64":"39660FC41AACDA31","md5":"2EF11C44DE597CD9A24DC435C2A594F8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":5,"Modified residue":1},"uniParcId":"UPI0005E75A21"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9UK61","uniProtkbId":"A0A0T9UK61_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34979.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"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"}],"value":"poxB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34979.1"}],"value":"ACZ76_16370"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00205"}]},{"type":"Domain","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":526,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]},{"type":"Region","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"FAD-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Region","location":{"start":{"value":532,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"Membrane-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":254,"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":274,"modifier":"EXACT"},"end":{"value":278,"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":292,"modifier":"EXACT"},"end":{"value":292,"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":407,"modifier":"EXACT"},"end":{"value":409,"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":434,"modifier":"EXACT"},"end":{"value":436,"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":434,"modifier":"EXACT"},"end":{"value":434,"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":461,"modifier":"EXACT"},"end":{"value":467,"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":461,"modifier":"EXACT"},"end":{"value":461,"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":466,"modifier":"EXACT"},"end":{"value":466,"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":"AKP34979.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"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"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34979.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34979.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34979.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619870.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000038.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9UK61","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61902562","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_16370","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9785953at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008289","properties":[{"key":"GoTerm","value":"F:lipid binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052737","properties":[{"key":"GoTerm","value":"F:pyruvate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048039","properties":[{"key":"GoTerm","value":"F:ubiquinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042867","properties":[{"key":"GoTerm","value":"P:pyruvate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02014","properties":[{"key":"EntryName","value":"TPP_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07039","properties":[{"key":"EntryName","value":"TPP_PYR_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1220:FF:000013","properties":[{"key":"EntryName","value":"Pyruvate dehydrogenase [ubiquinone]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000031","properties":[{"key":"EntryName","value":"Pyruvate dehydrogenase [ubiquinone]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000025","properties":[{"key":"EntryName","value":"Ubiquinone-dependent pyruvate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00850","properties":[{"key":"EntryName","value":"POX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR047211","properties":[{"key":"EntryName","value":"POXB-like"}]},{"database":"InterPro","id":"IPR044261","properties":[{"key":"EntryName","value":"Pyruvate_dehydrogenase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012000","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_cen_dom"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR000399","properties":[{"key":"EntryName","value":"TPP-bd_CS"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"InterPro","id":"IPR047212","properties":[{"key":"EntryName","value":"TPP_POXB-like"}]},{"database":"InterPro","id":"IPR047210","properties":[{"key":"EntryName","value":"TPP_PYR_POXB-like"}]},{"database":"NCBIfam","id":"NF006591","properties":[{"key":"EntryName","value":"poxB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981:SF2","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00205","properties":[{"key":"EntryName","value":"TPP_enzyme_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00187","properties":[{"key":"EntryName","value":"TPP_ENZYMES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKQTVATLVAKTLEQAGVKRIWGVTGDSLNGLSDSLHRMGTIEWMGTRHEEVAAFAAGAEAQLTGQLAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLEIAMRQAILNRGVSVIVLPGDVALQPAPEDAAVVWKTPKLPLVQPPMSELAILAQTLNKAKNITLMCGSGCADAHDEVVKLAEMLQAPVVHALRGKEHIEWDNPYSVGMTGLIGFSSGYHAMMNADTLLLLGTQFPYRAFYPTNANIIQIDINPGSIGAHCPVNMALVGDIQTTLRALLPQLAAKSDNKFLEKALEHYRTTRKELDGLATANDNQPIHPQYLAQQISRHATDDAIFTCDVGTPTVWAARYLAMNGKRRLLGSFNHGSMANAMPQAIGAQATAPERQVVALCGDGGFTMLMGDFLTLAQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGTDLHNPDFAAIANAAGIKGIRVEKASELDAALESAFAHPGPVLVDVVTAKQELSMPPQIKFEQAKGFSLYMLRAIINGRGDEVVELAKTNWLR","length":573,"molWeight":61756,"crc64":"D0F19160557BF113","md5":"783F2477864945CFAE1C76A39BB54848"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":9,"Site":1},"uniParcId":"UPI0005E49D90"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9UNW4","uniProtkbId":"A0A0T9UNW4_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-02-17","entryVersion":36,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33760.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33760.1"}],"value":"ACZ76_09495"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":397,"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":192,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"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":291,"modifier":"EXACT"},"end":{"value":291,"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":307,"modifier":"EXACT"},"end":{"value":310,"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":326,"modifier":"EXACT"},"end":{"value":326,"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":340,"modifier":"EXACT"},"end":{"value":340,"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":344,"modifier":"EXACT"},"end":{"value":344,"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":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"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":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"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":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33760.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33760.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33760.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618735.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000251.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9UNW4","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61903009","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_09495","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"FunFam","id":"3.40.50.10300:FF:000001","properties":[{"key":"EntryName","value":"Coenzyme A biosynthesis bifunctional protein CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1950:FF:000002","properties":[{"key":"EntryName","value":"Coenzyme A biosynthesis bifunctional protein CoaBC"},{"key":"MatchStatus","value":"1"}]},{"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":"MMTGLSGKHIVLGISGGIAAYKSPELVRRLRDRGAEVRVVMTTAAKAFITPLTLQAVSGYPVSDDLLDPTAEAAMGHIELGKWADLVIMAPATADLLARVAVGMANDLLTTLCLATAAPVAAVPAMNQQMYRAAATQANLQTLAHRGVLLWGPDSGSQACGDVGPGRMLDPLEIVALAHDHFSAKQDLQHLSVMITAGPTREALDPVRFISNQSSGKMGFAIAQAAAARGAKVTLVAGPVNLPTPAGVDRIDVVSALEMQQAVQNLAAQQNIFISCAAVADYRAEQVSDEKIKKQGDEITLKLVKNPDIVAGVASMAKNRPFVVGFAAETQNVEEYARQKLARKNLDLICANDVSLAEHGFNSDTNALHLFWLAGEKRLPLSDKHLLSQRLIDEIVSRYDEKNRH","length":405,"molWeight":43248,"crc64":"0B82B7003E746440","md5":"D41041A2451047CF9767CCB6FEBB3C08"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":6},"uniParcId":"UPI0005EA477C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9UP91","uniProtkbId":"A0A0T9UP91_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":45,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33792.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Bifunctional aspartokinase/homoserine dehydrogenase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Aspartokinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"2.7.2.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Homoserine dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"1.1.1.3"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33792.1"}],"value":"metL"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33792.1"}],"value":"metM"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33792.1"}],"value":"ACZ76_09665"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044938"}],"value":"Bifunctional aspartate kinase and homoserine dehydrogenase that catalyzes the first and the third steps toward the synthesis of lysine, methionine and threonine from aspartate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate + ATP = 4-phospho-L-aspartate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23776"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57535"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048561"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:23777"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048561"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + NAD(+) = L-aspartate 4-semialdehyde + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15757"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"1.1.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049031"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:15759"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049031"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + NADP(+) = L-aspartate 4-semialdehyde + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15761"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"1.1.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048841"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:15763"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048841"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"a metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001920"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:25213"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004766"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004986"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005062"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005139"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005056"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007952"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"In the C-terminal section; belongs to the homoserine dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010046"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"In the N-terminal section; belongs to the aspartokinase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"Aspartate/glutamate/uridylate kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00696"}]},{"type":"Domain","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":601,"modifier":"EXACT"}},"description":"Aspartate/homoserine dehydrogenase NAD-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03447"}]},{"type":"Domain","location":{"start":{"value":609,"modifier":"EXACT"},"end":{"value":804,"modifier":"EXACT"}},"description":"Homoserine dehydrogenase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00742"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"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"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023053"}],"id":"KW-0915","category":"Ligand","name":"Sodium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022697"}],"id":"KW-0791","category":"Biological process","name":"Threonine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33792.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33792.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33792.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618763.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000251.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9UP91","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61902975","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_09665","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9799110at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0004072","properties":[{"key":"GoTerm","value":"F:aspartate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004412","properties":[{"key":"GoTerm","value":"F:homoserine 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:0009090","properties":[{"key":"GoTerm","value":"P:L-homoserine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0009088","properties":[{"key":"GoTerm","value":"P:L-threonine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04257","properties":[{"key":"EntryName","value":"AAK_AK-HSDH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04892","properties":[{"key":"EntryName","value":"ACT_AK-like_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1160.10:FF:000009","properties":[{"key":"EntryName","value":"Bifunctional aspartokinase/homoserine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000124","properties":[{"key":"EntryName","value":"Bifunctional aspartokinase/homoserine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.1320","properties":[{"key":"EntryName","value":"Aspartokinase, catalytic domain"},{"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":"Gene3D","id":"3.30.2130.10","properties":[{"key":"EntryName","value":"VC0802-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR049638","properties":[{"key":"EntryName","value":"AK-HD"}]},{"database":"InterPro","id":"IPR041743","properties":[{"key":"EntryName","value":"AK-HSDH_N"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR005106","properties":[{"key":"EntryName","value":"Asp/hSer_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR001341","properties":[{"key":"EntryName","value":"Asp_kinase"}]},{"database":"InterPro","id":"IPR042199","properties":[{"key":"EntryName","value":"AsparK_Bifunc_asparK/hSer_DH"}]},{"database":"InterPro","id":"IPR018042","properties":[{"key":"EntryName","value":"Aspartate_kinase_CS"}]},{"database":"InterPro","id":"IPR011147","properties":[{"key":"EntryName","value":"Bifunc_Aspkin/hSer_DH"}]},{"database":"InterPro","id":"IPR001342","properties":[{"key":"EntryName","value":"HDH_cat"}]},{"database":"InterPro","id":"IPR019811","properties":[{"key":"EntryName","value":"HDH_CS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00657","properties":[{"key":"EntryName","value":"asp_kinases"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF007003","properties":[{"key":"EntryName","value":"metL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43070","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43070:SF5","properties":[{"key":"EntryName","value":"HOMOSERINE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00742","properties":[{"key":"EntryName","value":"Homoserine_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03447","properties":[{"key":"EntryName","value":"NAD_binding_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000727","properties":[{"key":"EntryName","value":"ThrA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00324","properties":[{"key":"EntryName","value":"ASPARTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01042","properties":[{"key":"EntryName","value":"HOMOSER_DHGENASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNATAVAAAVTGRQLHKFGGSSLADVKCYLRVANIMANYSHPGDLMVVSAAGSTTNQLISWLKLSQSDRLSAHQVQQNLRRYQHDLISGLLSPEMAEPLISEFIHDLERLAGLLDNKIDDATYAEVVGHGEIWSARLMAAVLNKLDMKASWLDARSFLRAERAAQPQIDEGRSYPLLQQLITQHPHQRLVVTGFISRNNAGETVLLGRNGSDYSATQVGALAGVERVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHTRTLQPVSGSDIDLQLRCSYQPEQGSTRIERVLASGSGAKIVTSHDDVCLIELQIAGHHDFSLAQKEIDLLLKRAQIKPLATGIHPDRNLLQLCYTSEVVNSALRVLEDATLPGRLSLREGLALVALVGAGVSKNPLHSHRFYQQLKDQPVEFIWQAEDGISLVAVLRLGPTEHLIQGLHQSLFRAEKRIGLVLFGKGNIGARWLELFAREQKNISARSGFEFVLAGVVDSRRSLLSYDGLDASRTLAFYDDEAIEQDEESLFLWMRAHPFDDLVVLDVTASESLAEQYLDFASYGFHVVSANKLAGASSSNNYRQIRDAFAKTGRHWLYNATVGAGLPVNHTVRDLRDSGDSILAISGIFSGTLSWLFLQFDGTVPFTELVDQAWQQGLTEPDPRVDLSGQDVMRKLVILAREAGYDIEPNQVRVESLVPAGADVGSVDQFFENGEALNQQMVQRLEAANEMGLVLRYVARFDANGKARVGVEAVRADHPLASLLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDLNRLSQLL","length":811,"molWeight":89105,"crc64":"904B3CD558D3CC27","md5":"BD292C6DB9DE93067A199A276F15AA68"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SIMILARITY":2},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0005E17139"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9UR35","uniProtkbId":"A0A0T9UR35_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":48,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32746.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Flavohemoprotein"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Flavohemoglobin"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Hemoglobin-like protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Nitric oxide dioxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"NO oxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"NOD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"1.14.12.17"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"hmp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32746.1"}],"value":"ACZ76_03870"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025094"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 nitric oxide + NADH + 2 O2 = 2 nitrate + NAD(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19469"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16480"},{"database":"ChEBI","id":"CHEBI:17632"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.14.12.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048649"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 nitric oxide + NADPH + 2 O2 = 2 nitrate + NADP(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19465"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16480"},{"database":"ChEBI","id":"CHEBI:17632"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.14.12.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049433"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008414"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Belongs to the globin family. Two-domain flavohemoproteins subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006401"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"Globin","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS01033"}]},{"type":"Domain","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"FAD-binding FR-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51384"}]},{"type":"Region","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"Reductase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Active site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Active site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"proximal binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Involved in heme-bound ligand stabilization and O-O bond activation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Influences the redox potential of the prosthetic heme and FAD groups","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Influences the redox potential of the prosthetic heme and FAD groups","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022575"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0216","category":"Biological process","name":"Detoxification"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000356"}],"id":"KW-0561","category":"Biological process","name":"Oxygen transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000356"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32746.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32746.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP32746.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048616982.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000179.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9UR35","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61903548","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_03870","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801223at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0071949","properties":[{"key":"GoTerm","value":"F:FAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008941","properties":[{"key":"GoTerm","value":"F:nitric oxide dioxygenase [NAD(P)H] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019825","properties":[{"key":"GoTerm","value":"F:oxygen binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005344","properties":[{"key":"GoTerm","value":"F:oxygen carrier activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071500","properties":[{"key":"GoTerm","value":"P:cellular response to nitrosative stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046210","properties":[{"key":"GoTerm","value":"P:nitric oxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06184","properties":[{"key":"EntryName","value":"flavohem_like_fad_nad_binding"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd14776","properties":[{"key":"EntryName","value":"HmpEc-globin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.490.10:FF:000003","properties":[{"key":"EntryName","value":"Flavohemoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000034","properties":[{"key":"EntryName","value":"Flavohemoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.80:FF:000010","properties":[{"key":"EntryName","value":"Flavohemoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.490.10","properties":[{"key":"EntryName","value":"Globins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.80","properties":[{"key":"EntryName","value":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01252","properties":[{"key":"EntryName","value":"Hmp"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008333","properties":[{"key":"EntryName","value":"Cbr1-like_FAD-bd_dom"}]},{"database":"InterPro","id":"IPR017927","properties":[{"key":"EntryName","value":"FAD-bd_FR_type"}]},{"database":"InterPro","id":"IPR001709","properties":[{"key":"EntryName","value":"Flavoprot_Pyr_Nucl_cyt_Rdtase"}]},{"database":"InterPro","id":"IPR039261","properties":[{"key":"EntryName","value":"FNR_nucleotide-bd"}]},{"database":"InterPro","id":"IPR000971","properties":[{"key":"EntryName","value":"Globin"}]},{"database":"InterPro","id":"IPR009050","properties":[{"key":"EntryName","value":"Globin-like_sf"}]},{"database":"InterPro","id":"IPR012292","properties":[{"key":"EntryName","value":"Globin/Proto"}]},{"database":"InterPro","id":"IPR023950","properties":[{"key":"EntryName","value":"Hmp"}]},{"database":"InterPro","id":"IPR001433","properties":[{"key":"EntryName","value":"OxRdtase_FAD/NAD-bd"}]},{"database":"InterPro","id":"IPR017938","properties":[{"key":"EntryName","value":"Riboflavin_synthase-like_b-brl"}]},{"database":"NCBIfam","id":"NF009805","properties":[{"key":"EntryName","value":"hmpA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43396","properties":[{"key":"EntryName","value":"FLAVOHEMOPROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43396:SF3","properties":[{"key":"EntryName","value":"FLAVOHEMOPROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00970","properties":[{"key":"EntryName","value":"FAD_binding_6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00042","properties":[{"key":"EntryName","value":"Globin"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00175","properties":[{"key":"EntryName","value":"NAD_binding_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00371","properties":[{"key":"EntryName","value":"FPNCR"}]},{"database":"PRINTS","id":"PR00410","properties":[{"key":"EntryName","value":"PHEHYDRXLASE"}]},{"database":"SUPFAM","id":"SSF52343","properties":[{"key":"EntryName","value":"Ferredoxin reductase-like, C-terminal NADP-linked domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46458","properties":[{"key":"EntryName","value":"Globin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63380","properties":[{"key":"EntryName","value":"Riboflavin synthase domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51384","properties":[{"key":"EntryName","value":"FAD_FR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01033","properties":[{"key":"EntryName","value":"GLOBIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLDRQTIATVQSTIPLLAATGPKVTAHFYDRMFEHNPELKHIFNMSNQINGDQREALFNALCAYAINIDNLAALLPAVERIAQKHTSLNIQPEHYAIVGHHLICTLDEMFSPGQEVLDAWGKAYGVLADVFIQRESQIYQQGETSTGGWRTLRRFRIIKKEMQSEVICSFVLAPEDGGRVLDFKPGQYLGIYIEDERLEYQEIRQYSLTAAPNGQTYRIAVKREEQGTVSNYLHQQLNEGDNVRIAPPRGDFFLNVSPDTPVALISAGVGQTPMLSMLNTLYDQQHAASVHWLHAAENGRVHAFADEVTTIATKMPNLSRHVWYREPTAQDNHGEDYHSEGLMDLSSHQWLAADPNRHYYFCGPLAFMQFAGRQLLAQGVASERIHYECFGPHKVI","length":396,"molWeight":44779,"crc64":"B2B684972024780A","md5":"1BD12E439C42DD88FB3B4CF2BE2692D2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"DOMAIN":1,"SIMILARITY":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":2,"Binding site":5,"Site":3},"uniParcId":"UPI0005DEB360"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9UUD8","uniProtkbId":"A0A0T9UUD8_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":49,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33666.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"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":"AKP33666.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33666.1"}],"value":"ACZ76_08980"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Domain","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Mannose-1-phosphate guanyltransferase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF25087"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":14,"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":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":82,"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":103,"modifier":"EXACT"},"end":{"value":105,"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":105,"modifier":"EXACT"},"end":{"value":105,"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":140,"modifier":"EXACT"},"end":{"value":140,"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":154,"modifier":"EXACT"},"end":{"value":154,"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":169,"modifier":"EXACT"},"end":{"value":169,"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":227,"modifier":"EXACT"},"end":{"value":227,"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":227,"modifier":"EXACT"},"end":{"value":227,"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":333,"modifier":"EXACT"},"end":{"value":333,"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":351,"modifier":"EXACT"},"end":{"value":351,"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":366,"modifier":"EXACT"},"end":{"value":366,"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":377,"modifier":"EXACT"},"end":{"value":377,"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":380,"modifier":"EXACT"},"end":{"value":380,"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":386,"modifier":"EXACT"},"end":{"value":387,"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":405,"modifier":"EXACT"},"end":{"value":405,"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":423,"modifier":"EXACT"},"end":{"value":423,"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":440,"modifier":"EXACT"},"end":{"value":440,"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":"UP000069914"}],"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":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33666.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33666.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33666.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618627.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000234.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9UUD8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61903972","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_08980","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9775031at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.160.10.10:FF:000011","properties":[{"key":"EntryName","value":"Bifunctional protein GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.550.10:FF:000006","properties":[{"key":"EntryName","value":"Bifunctional protein GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR056729","properties":[{"key":"EntryName","value":"GMPPB_C"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"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":"NF006986","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":"PF25087","properties":[{"key":"EntryName","value":"GMPPB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNSSMSVVILAAGKGTRMYSDLPKVLHPLAGKPMVQHVIDAAMKLGAENVHLVYGHGGELLKKALSDPSLNWVLQAEQLGTGHAMQQAAPHFADDEDVLMLYGDVPLISVDTLQRLLAAKPQGGIGLLTVKLDDPSGYGRIVRENGDVVGIVEHKDASDAQREINEINTGILVANGRDLKRWLSRLDNNNAQGEFYITDIIAMAHADGQKIATVHPTRLSEVEGVNNRLQLATLERVFQSEQAEKLLLAGVMLLDPARFDLRGELTHGRDITIDTNVIIEGHVTLGDRVRIGTGCVLKSCVIGDDSEISPYTVLENSRLDAGCTVGPFARLRPGAELAEGAHVGNFVEIKNTRLGKGSKAGHLSYLGDAEIGSGVNIGAGTITCNYDGANKFKTIIGDNVFVGSDTQLVAPVTVANGVTIAAGTTVTRDIAEDELVLSRVKQVHVQGWQRPVKKK","length":456,"molWeight":48828,"crc64":"8A15B0CAF1C919FE","md5":"E72A46E0A9B7D841872D9EFACB1BB3D6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI0005DBB4EE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0T9UWV9","uniProtkbId":"A0A0T9UWV9_YERAE","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":47,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34362.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34362.1"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34362.1"}],"value":"ACZ76_12850"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":515,"modifier":"EXACT"},"end":{"value":515,"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":517,"modifier":"EXACT"},"end":{"value":517,"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":14,"modifier":"EXACT"},"end":{"value":14,"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":14,"modifier":"EXACT"},"end":{"value":14,"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":15,"modifier":"EXACT"},"end":{"value":20,"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":72,"modifier":"EXACT"},"end":{"value":72,"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":72,"modifier":"EXACT"},"end":{"value":72,"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":140,"modifier":"EXACT"},"end":{"value":140,"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":147,"modifier":"EXACT"},"end":{"value":149,"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":187,"modifier":"EXACT"},"end":{"value":192,"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":187,"modifier":"EXACT"},"end":{"value":192,"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":223,"modifier":"EXACT"},"end":{"value":223,"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":223,"modifier":"EXACT"},"end":{"value":223,"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":239,"modifier":"EXACT"},"end":{"value":241,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":380,"modifier":"EXACT"},"end":{"value":383,"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":403,"modifier":"EXACT"},"end":{"value":403,"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":470,"modifier":"EXACT"},"end":{"value":470,"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":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34362.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34362.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34362.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619264.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHPU010000066.1"}]},{"database":"AlphaFoldDB","id":"A0A0T9UWV9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61904271","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_12850","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPTQHGEVFVTEDGAETDLDLGHYERFIRTKMTRRNNFTTGRIYSEVLRKERRGDYLGATIQVIPHITNAIKERIIEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAVDVGREHTLYMHLTLVPYLAAAGEVKTKPTQHSVKELLSIGIQPDVLICRSDRPVPANERAKIALFCNVPEKAVISLKDVDSIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVLYEESNPGGEVTIGMIGKYVELPDAYKSVIEALKHGGLKNRLTVNIKLIDSQDVETRGEEMLKGLDAILIPGGFGYRGVEGMVLTANYAREHNIPYLGICLGMQVALLEFARNVVGMENANSTEFVPDCKYPVVALITEWRDEDGNVEVRSEESDLGGTMRVGGQPCNLTEGSLVRQMYGEPIIVERHRHRYEVNNMLLKQIEAAGLRVAGRSADNKLVEIIELPDHPWFVACQFHPEFTSTPRDGHPLFAGFVKAAGDYQKRQVK","length":545,"molWeight":60248,"crc64":"18F6D81D8EF1DA3A","md5":"01638108DA4F1340BEC5707F279346FA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":16},"uniParcId":"UPI0005E5B288"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UAG0","uniProtkbId":"A0ABM5UAG0_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32553.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Fatty acid oxidation complex subunit alpha"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"4.2.1.17"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"5.1.2.3"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"3-hydroxyacyl-CoA dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"1.1.1.35"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32553.1"}],"value":"fadJ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32553.1"}],"value":"ACZ76_02780"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21760"},{"database":"ChEBI","id":"CHEBI:57315"},{"database":"ChEBI","id":"CHEBI:57316"}],"ecNumber":"5.1.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22432"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:90726"}],"ecNumber":"1.1.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049556"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16105"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:58856"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20724"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:137480"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005005"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008750"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007005"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00378"}]},{"type":"Domain","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase NAD binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02737"}]},{"type":"Domain","location":{"start":{"value":511,"modifier":"EXACT"},"end":{"value":604,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Domain","location":{"start":{"value":642,"modifier":"EXACT"},"end":{"value":726,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]},{"type":"Region","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":745,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]},{"type":"Site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]},{"type":"Site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022963"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"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_01617"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32553.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32553.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP32553.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048616612.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQI010000018.1"}]},{"database":"GeneID","id":"61901517","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_02780","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008692","properties":[{"key":"GoTerm","value":"F:3-hydroxybutyryl-CoA epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004300","properties":[{"key":"GoTerm","value":"F:enoyl-CoA hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016509","properties":[{"key":"GoTerm","value":"F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070403","properties":[{"key":"GoTerm","value":"F:NAD+ binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006635","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1040.50:FF:000003","properties":[{"key":"EntryName","value":"Fatty acid oxidation complex subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000011","properties":[{"key":"EntryName","value":"Fatty acid oxidation complex subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000009","properties":[{"key":"EntryName","value":"Fatty oxidation complex, alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1040.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01617","properties":[{"key":"EntryName","value":"FadJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006180","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR006176","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR006108","properties":[{"key":"EntryName","value":"3HC_DH_C"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR001753","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra/iso"}]},{"database":"InterPro","id":"IPR050136","properties":[{"key":"EntryName","value":"FA_oxidation_alpha_subunit"}]},{"database":"InterPro","id":"IPR012802","properties":[{"key":"EntryName","value":"FadJ"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF008363","properties":[{"key":"EntryName","value":"fadJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02440","properties":[{"key":"EntryName","value":"FadJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612:SF3","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00725","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02737","properties":[{"key":"EntryName","value":"3HCDH_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00067","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKEKALNSVAEPIVVDTATATPSVFSLAVRPDNIGVITIDVIGDKVNTLKAEFAEQIADILQKAQALPHLQGLVIISGKPDSFIAGADITMIAACRSAQDARKLAQKGQSILAQIAAFPVPVVAAIHGACLGGGLELALACHSRICSLDDKTVLGLPEVQLGLLPGSGGTQRLPRLVGVSKALDMILTGRQVRARQAVKMGLVDDAVPQDILLDVAIERAKAGWLDKPVVPWQERLLSGPLGKTLLFNIVRKKTLAKTKGHYPAAERIIDVVRKGLDHGSASGYEAEATAFGELAMSPQSAALRSLFFATTSLKKETGGDAQPRAIHRVGVLGGGLMGGGIANVTATRAGLPVRIKDINPQGINQALKYTWDALGKRVRSKRMRPAERQRQMMLISGSTDYRGFDTVDLVIEAVFEDLSLKQQMVADIERFGAAHTIFASNTSSLPISQIAAQAQRPEQVIGLHYFSPVDKMPLVEVIPHAKTSEETIATTVALARKQGKTAIVVADRAGFYVNRILAPYINEAARCLLDGEPIDSIDSSLVDFGFPVGPITLLDEVGIDVGTKIMPILVEQLGPRFAAPPSFDVILQDGRKGRKNGRGFYLYPTQSRGLKWKRNPGKQVDASVYVLLGVTPKAHLGSAVIAQRCTMMMLNEAVRCLDESIIRNPRDGDIGAVFGIGFPPFLGGPFRYLDSLGADKVVKTLRLLAQQYGERFEPCPLLVTMAEQQQRFYPDENSENVASDNAPI","length":745,"molWeight":80127,"crc64":"A0F98BAFC78BE254","md5":"2EC5EB52981D52DB1FA1D486556F0A45"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2},"countByFeatureType":{"Domain":4,"Region":2,"Site":2},"uniParcId":"UPI0005E7652C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UAQ7","uniProtkbId":"A0ABM5UAQ7_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32906.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"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":"AKP32906.1"}],"value":"recB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32906.1"}],"value":"ACZ76_04785"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51198"}]},{"type":"Domain","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":746,"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":854,"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":903,"modifier":"EXACT"},"end":{"value":1203,"modifier":"EXACT"}},"description":"Nuclease activity, interacts with RecD and RecA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Coiled coil","location":{"start":{"value":782,"modifier":"EXACT"},"end":{"value":809,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Active site","location":{"start":{"value":1093,"modifier":"EXACT"},"end":{"value":1093,"modifier":"EXACT"}},"description":"For nuclease activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":31,"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":969,"modifier":"EXACT"},"end":{"value":969,"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":1080,"modifier":"EXACT"},"end":{"value":1080,"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":1093,"modifier":"EXACT"},"end":{"value":1093,"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":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"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":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32906.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32906.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP32906.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048617281.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000016.1"}]},{"database":"GeneID","id":"61903817","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_04785","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"CDD","id":"cd18807","properties":[{"key":"EntryName","value":"SF1_C_UvrD"},{"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":"Gene3D","id":"1.10.3170.10","properties":[{"key":"EntryName","value":"Recbcd, chain B, domain 2"},{"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":"NCBIfam","id":"NF008128","properties":[{"key":"EntryName","value":"recB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00609","properties":[{"key":"EntryName","value":"recB"},{"key":"MatchStatus","value":"1"}]},{"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":"MTSMTPQRLEPLTLPLYGERLIEASAGTGKTFTIGVLYLRLLLGLGGGAAFSRPLMVEDILVVTFTEAATEELRGRIRDNIHELRIACVRGVSDNPMHKALLAEIIDLSEAAAQLLAAERQMDEAAIYTIHGFCQRMLANNAFESGILFEQTLVQDELPLRRQACADFWRRHCYPLPLAVARAVSQEWSGPEALLKDLSAYLQGETPKFRQAPGDDETILSRHQQIVVQIDAVKAQWCAAAPELEALISISGVDKRSYSARYLPNWLEKVGAWADQETGDYQLPKELEKFRQSVLFEKTKKGTAPQHALFSAIDSLFEQPLTLRDLILARAISEIRTSVQQEKRQRAELGFDDLLSKLDVALQQSGGELLAQSIRNRYPVAMIDEFQDTDPQQYRIFHTLYGGQKECGLLLIGDPKQAIYAFRGADIFTYIRARSEVSAHYTLETNWRSSFPMVQSVNRLFSLVEVPFLFEQIPFIKVSAAEKNSHLSFEIKGKKQPAISFWLQPGEGVGVSEYQQLMARQCAAQIRDWLTAGQNGQAQLVTADGSRPVQASDITILVRSRAEAALVRDAMSALAIPSVYLSNRDSVFDTAEAKDLLWLLQAVLAPEQERALRSAMATGMLGLDAKILDALNHDERAWDALVEEFDSYRQHWQRRGVLPMLREIMAHRHLAENLLATPGGERRLTDVLHLGELLQEAASQLDSEHALIRWLAQQIAQPNHQSDNQQLRLESDRHLVQVITIHKSKGLEYPLVWLPFVGNFRQQQDVLYHDRHSFEALLDLNADEESQALAEEERLAEDLRLLYVALTRAVYHCSVGIAPLIKGGRKKQGESDMHRSALGYLVQQGQAGDAQYLADKLAELTAAAKGDISVSLAERPDDTPWQPQPEILPALAARQFNRQIQDYWRVTSYSGLQQHGSSKGGASQTLNVPLQELLPRLDTDAVGEQVLIATAHLTPHTFPRGAAPGTFLHDLLEPMDFSQPIEQEWLAEQLQRQGFGEQWLPMLSQWLNDIVQVPLNTTGVTLAGLTPESKQAELQFYLPIDTLLRASELDSLIKHYDPLSRQCPVLDFQQVRGMLKGFIDLVFCWQGKYYLLDYKSNWLGEDSSAYTREAMTQAMAEHRYDLQYQLYTLALHRYLRHRLADYDYQRDFGGVIYLFLRGVNKQHPGNGIFSCRPELELIEGMDCLFSGREINDNAIQVDERASL","length":1203,"molWeight":135613,"crc64":"65636FBB7960A76D","md5":"363E5C66C96A7291A5F04037F31ECFEB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":2,"Coiled coil":1,"Active site":1,"Binding site":4},"uniParcId":"UPI0005E7D101"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UCC5","uniProtkbId":"A0ABM5UCC5_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33480.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Siroheme synthase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Uroporphyrinogen-III C-methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Urogen III methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"2.1.1.107"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"SUMT"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Uroporphyrinogen III methylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"UROM"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Precorrin-2 dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"1.3.1.76"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Sirohydrochlorin ferrochelatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"4.99.1.4"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33480.1"}],"value":"cysG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33480.1"}],"value":"ACZ76_08000"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"precorrin-2 + NAD(+) = sirohydrochlorin + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58351"},{"database":"ChEBI","id":"CHEBI:58827"}],"ecNumber":"1.3.1.76","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047561"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"siroheme + 2 H(+) = sirohydrochlorin + Fe(2+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24360"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:58351"},{"database":"ChEBI","id":"CHEBI:60052"}],"ecNumber":"4.99.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrinogen III + 2 S-adenosyl-L-methionine = precorrin-2 + 2 S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32459"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57308"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:58827"},{"database":"ChEBI","id":"CHEBI:59789"}],"ecNumber":"2.1.1.107","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060548"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025705"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005010"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005879"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003960"}],"value":"Belongs to the precorrin methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"In the C-terminal section; belongs to the precorrin methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Siroheme synthase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14824"}]},{"type":"Domain","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Sirohaem synthase dimerisation","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10414"}]},{"type":"Domain","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"Tetrapyrrole methylase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00590"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]},{"type":"Region","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Uroporphyrinogen-III C-methyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]},{"type":"Active site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR036426-1"}]},{"type":"Active site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR036426-1"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Modified residue","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022573"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0169","category":"Biological process","name":"Cobalamin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"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_01646"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"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_01646"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33480.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP33480.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP33480.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048618305.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000357.1"}]},{"database":"GeneID","id":"61902019","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_08000","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043115","properties":[{"key":"GoTerm","value":"F:precorrin-2 dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004325","properties":[{"key":"GoTerm","value":"F:protoporphyrin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051266","properties":[{"key":"GoTerm","value":"F:sirohydrochlorin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004851","properties":[{"key":"GoTerm","value":"F:uroporphyrin-III C-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009236","properties":[{"key":"GoTerm","value":"P:cobalamin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019354","properties":[{"key":"GoTerm","value":"P:siroheme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd11642","properties":[{"key":"EntryName","value":"SUMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.160.110:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.950.10:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1010.10:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000092","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1010.10","properties":[{"key":"EntryName","value":"Cobalt-precorrin-4 Transmethylase, Domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.950.10","properties":[{"key":"EntryName","value":"Methyltransferase, Cobalt-precorrin-4 Transmethylase, 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":"Gene3D","id":"1.10.8.210","properties":[{"key":"EntryName","value":"Sirohaem synthase, dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.160.110","properties":[{"key":"EntryName","value":"Siroheme synthase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01646","properties":[{"key":"EntryName","value":"Siroheme_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000878","properties":[{"key":"EntryName","value":"4pyrrol_Mease"}]},{"database":"InterPro","id":"IPR035996","properties":[{"key":"EntryName","value":"4pyrrol_Methylase_sf"}]},{"database":"InterPro","id":"IPR014777","properties":[{"key":"EntryName","value":"4pyrrole_Mease_sub1"}]},{"database":"InterPro","id":"IPR014776","properties":[{"key":"EntryName","value":"4pyrrole_Mease_sub2"}]},{"database":"InterPro","id":"IPR006366","properties":[{"key":"EntryName","value":"CobA/CysG_C"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR050161","properties":[{"key":"EntryName","value":"Siro_Cobalamin_biosynth"}]},{"database":"InterPro","id":"IPR037115","properties":[{"key":"EntryName","value":"Sirohaem_synt_dimer_dom_sf"}]},{"database":"InterPro","id":"IPR012409","properties":[{"key":"EntryName","value":"Sirohaem_synth"}]},{"database":"InterPro","id":"IPR028281","properties":[{"key":"EntryName","value":"Sirohaem_synthase_central"}]},{"database":"InterPro","id":"IPR019478","properties":[{"key":"EntryName","value":"Sirohaem_synthase_dimer_dom"}]},{"database":"InterPro","id":"IPR006367","properties":[{"key":"EntryName","value":"Sirohaem_synthase_N"}]},{"database":"InterPro","id":"IPR003043","properties":[{"key":"EntryName","value":"Uropor_MeTrfase_CS"}]},{"database":"NCBIfam","id":"TIGR01469","properties":[{"key":"EntryName","value":"cobA_cysG_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF007922","properties":[{"key":"EntryName","value":"cysG"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01470","properties":[{"key":"EntryName","value":"cysG_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004790","properties":[{"key":"EntryName","value":"PRK06136.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45790:SF1","properties":[{"key":"EntryName","value":"SIROHEME SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45790","properties":[{"key":"EntryName","value":"SIROHEME SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10414","properties":[{"key":"EntryName","value":"CysG_dimeriser"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13241","properties":[{"key":"EntryName","value":"NAD_binding_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14824","properties":[{"key":"EntryName","value":"Sirohm_synth_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00590","properties":[{"key":"EntryName","value":"TP_methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF036426","properties":[{"key":"EntryName","value":"Sirohaem_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75615","properties":[{"key":"EntryName","value":"Siroheme synthase middle domains-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53790","properties":[{"key":"EntryName","value":"Tetrapyrrole methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00839","properties":[{"key":"EntryName","value":"SUMT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00840","properties":[{"key":"EntryName","value":"SUMT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDYFPIFCQLQNKACLLVGGGEVAERKARLLLEAGAVVTANACEFTPQFHDWAEQGRLSLVSSEFVPELLAEKWLVIAATDQVAVNALVYQSANQQRVFCNVVDDPKRTSFIMPSIIDRSPIMIAISSGGKAPVLARLLREKLEAILPLHLGQLAQLAGDLRQRVKQHFAAMPDRRRFWEKLLTHDRLAQSLANDDQMQVEQHIEQLFNAPLSDRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDEVMNLVRRDAERIFVGKQSGHHSVPQDQINQILLQQAQLGKRVVRLKGGDPFIFGRGGEELETLAEYGIPFSVVPGITAASGCSAYSGIPLTHRDHAQSVRLITGHAKKEAQLDWANLAAEKQTLVFYMGLSQAGEIQQQLIRHGMPAATPVALVENGTSRHQRVVSGELSQLALLSQQVSSPSLIIVGSVVSLREKLNWFSSAEHGKVAVKEQAERVG","length":472,"molWeight":51749,"crc64":"DA1ACDDA2F6D04AB","md5":"61F296498EDBBBAE8D08614CCDA6E915"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"PATHWAY":5,"SIMILARITY":3},"countByFeatureType":{"Domain":3,"Region":2,"Active site":2,"Binding site":8,"Modified residue":1},"uniParcId":"UPI0005E098B3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UE35","uniProtkbId":"A0ABM5UE35_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34105.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34105.1"}],"value":"hflB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34105.1"}],"value":"ftsH"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34105.1"}],"value":"ACZ76_11435"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":592,"modifier":"EXACT"},"end":{"value":651,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":630,"modifier":"EXACT"},"end":{"value":643,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34105.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34105.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34105.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619040.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABHQD010000287.1"}]},{"database":"GeneID","id":"61901262","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_11435","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.720.210:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.720.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"NF008004","properties":[{"key":"EntryName","value":"ftsH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076:SF97","properties":[{"key":"EntryName","value":"ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076","properties":[{"key":"EntryName","value":"METALLOPROTEASE M41 FTSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFMSDVTQEQVREARINGREINVSKKDNSKYTTFIPVNDPKLLDTLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTSFADVAGCDEAKEEVSELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLDTDIDASVIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEKVSTGASNDIKVATSIARNMVTQWGFSEKLGPLLYAEEEGEIFLGRSVAKAKHMSDETARIIDQEVKLLIERNYQRARKLLLENMDVLHSMKDALMKYETIDAPQIDDLMNRKEVRPPAGWDNATKAKSSDNDSTPKAPTAVEEPHTPTSGNTTPGNTNSMPEQLGDK","length":651,"molWeight":71436,"crc64":"06EFB4F74103E2D2","md5":"37B32593601DA9EB87595D2A48DBE807"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":4},"uniParcId":"UPI00065DEE28"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABM5UER3","uniProtkbId":"A0ABM5UER3_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34348.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018637"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR02071"}],"value":"Penicillin-binding protein 1B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"PBP-1b"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"PBP1b"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032454"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"Murein polymerase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34348.1"}],"value":"mrcB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34348.1"}],"value":"ponB"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34348.1"}],"value":"ACZ76_12760"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002624"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.","ecNumber":"3.4.16.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans,octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23708"},{"database":"Rhea","id":"RHEA-COMP:9602"},{"database":"Rhea","id":"RHEA-COMP:9603"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58405"},{"database":"ChEBI","id":"CHEBI:60033"},{"database":"ChEBI","id":"CHEBI:78435"}],"ecNumber":"2.4.99.28","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049902"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060592"}],"value":"Glycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004533"}],"value":"Cell inner membrane","id":"SL-0037"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"In the C-terminal section; belongs to the transpeptidase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007739"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"value":"In the N-terminal section; belongs to the glycosyltransferase 51 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Transglycosylase PBP1b N-terminal transmembrane","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14812"}]},{"type":"Domain","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"Bifunctional transglycosylase second","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14814"}]},{"type":"Domain","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"Glycosyl transferase family 51","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00912"}]},{"type":"Domain","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":724,"modifier":"EXACT"}},"description":"Penicillin-binding protein transpeptidase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00905"}]},{"type":"Domain","location":{"start":{"value":768,"modifier":"EXACT"},"end":{"value":804,"modifier":"EXACT"}},"description":"Penicillin-binding protein 1B C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF30367"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Proton donor; for transglycosylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002799-1"}]},{"type":"Active site","location":{"start":{"value":518,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"Acyl-ester intermediate; for transpeptidase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002799-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023251"}],"id":"KW-0046","category":"Biological process","name":"Antibiotic resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022645"}],"id":"KW-0121","category":"Molecular function","name":"Carboxypeptidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022519"}],"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002799"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34348.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP34348.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP34348.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048619252.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000023.1"}]},{"database":"GeneID","id":"61904253","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_12760","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0030288","properties":[{"key":"GoTerm","value":"C:outer membrane-bounded periplasmic space"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009274","properties":[{"key":"GoTerm","value":"C:peptidoglycan-based cell wall"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008658","properties":[{"key":"GoTerm","value":"F:penicillin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008955","properties":[{"key":"GoTerm","value":"F:peptidoglycan glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009002","properties":[{"key":"GoTerm","value":"F:serine-type D-Ala-D-Ala carboxypeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0071555","properties":[{"key":"GoTerm","value":"P:cell wall organization"},{"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:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046677","properties":[{"key":"GoTerm","value":"P:response to antibiotic"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.3810.10:FF:000002","properties":[{"key":"EntryName","value":"Penicillin-binding protein 1B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.710.10:FF:000006","properties":[{"key":"EntryName","value":"Penicillin-binding protein 1B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3810.10","properties":[{"key":"EntryName","value":"Biosynthetic peptidoglycan transglycosylase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.100","properties":[{"key":"EntryName","value":"Cytochrome c1, transmembrane anchor, C-terminal"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.710.10","properties":[{"key":"EntryName","value":"DD-peptidase/beta-lactamase superfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.2060.10","properties":[{"key":"EntryName","value":"Penicillin-binding protein 1b domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012338","properties":[{"key":"EntryName","value":"Beta-lactam/transpept-like"}]},{"database":"InterPro","id":"IPR001264","properties":[{"key":"EntryName","value":"Glyco_trans_51"}]},{"database":"InterPro","id":"IPR050396","properties":[{"key":"EntryName","value":"Glycosyltr_51/Transpeptidase"}]},{"database":"InterPro","id":"IPR023346","properties":[{"key":"EntryName","value":"Lysozyme-like_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR063152","properties":[{"key":"EntryName","value":"PBP1b_C"}]},{"database":"InterPro","id":"IPR032730","properties":[{"key":"EntryName","value":"PBP1b_TM"}]},{"database":"InterPro","id":"IPR011813","properties":[{"key":"EntryName","value":"PBP_1b"}]},{"database":"InterPro","id":"IPR001460","properties":[{"key":"EntryName","value":"PCN-bd_Tpept"}]},{"database":"InterPro","id":"IPR036950","properties":[{"key":"EntryName","value":"Transglycosylase"}]},{"database":"InterPro","id":"IPR028166","properties":[{"key":"EntryName","value":"UB2H"}]},{"database":"NCBIfam","id":"NF007061","properties":[{"key":"EntryName","value":"mrcB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02071","properties":[{"key":"EntryName","value":"PBP_1b"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32282","properties":[{"key":"EntryName","value":"BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32282:SF11","properties":[{"key":"EntryName","value":"PENICILLIN-BINDING PROTEIN 1B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14812","properties":[{"key":"EntryName","value":"PBP1_TM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF30367","properties":[{"key":"EntryName","value":"PBP1b_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00912","properties":[{"key":"EntryName","value":"Transgly"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00905","properties":[{"key":"EntryName","value":"Transpeptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14814","properties":[{"key":"EntryName","value":"UB2H"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002799","properties":[{"key":"EntryName","value":"PBP_1b"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56601","properties":[{"key":"EntryName","value":"beta-lactamase/transpeptidase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53955","properties":[{"key":"EntryName","value":"Lysozyme-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGDDREPIGRKGKKAQPKAAPKRPLRRRRDEDEYEDEDYLDDEEHDDDDYDDEEEPMPRKVASRPPRKKRRWLGLFIKLFLVGAVVLAIYGVYLDSQIRSRIDGKVWQLPAAVYGRMVNLEPGMSYSKKEMVDLLEGMQYRQVTRMTRPGEFTVQGDSIDILRRPFDFPDAKEGQIRARLVFRDDRLVQIQNLDNQRDFGFLRLDPKLITMLQSPNGEQRLFVPRAGFPDLLVDTLLATEDRHFYEHDGISPYSIGRAMLANLTAGKAVQGGSTLTQQLVKNLFLTNERSLWRKANEAYMALLVDYRYSKDRILELYLNEVYLGQSGSDQIRGFPLASLYYFGRPVNELSLDQQAMLVGMVKGASLYNPWRNPTLALERRNLVLRLLQNQGVIDAELYTMLSARPLGVQPKGGVITPQPAFMQMVRQELQQKLGDKINDLSGVKIFTTLDPVSQDAAEKAIEDGIPALKAARHLDDLEAAMVIVDRFSGEVRAMVGGAQPQYAGFNRAMQARRLVGSLAKPPTYLTALSEPDKFRLNTWLADQPLSIKLPNGSLWQPKNYDRQYRGQVMLVDALANSLNVPTVNLGMSVGLDQITAMLQRLGIPKAVINPVPAMLLGAIDLTPVEVAQEYQTIASGGNRAPLSAVRSVIAEDGTVLYQSFPQAERMVPAQAAYLTLYAMQQGVARGTSRSLSVKFSKYNLAAKTGTTNDLRDSWFAGIDGKEVAIAWVGRDNNGPAKLTGANGALTLYRRYLENQTPLPLVLQPPEGISQMNIDSAGNFVCGDGGGMRSIPVWTENPQGLCQAAAPTEQPKADGDGVAGWIKDMFGQ","length":828,"molWeight":92160,"crc64":"97FA1568DAAEBACC","md5":"D9836DF02E10709D249CE3A64B96AE77"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":2},"countByFeatureType":{"Transmembrane":1,"Domain":5,"Region":1,"Compositional bias":3,"Active site":2},"uniParcId":"UPI0005E49A75"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABN4H2W1","uniProtkbId":"A0ABN4H2W1_YERAE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Yersinia aleksiciae","taxonId":263819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32722.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32722.1"}],"value":"ACZ76_03750"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"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":143,"modifier":"EXACT"},"end":{"value":143,"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":146,"modifier":"EXACT"},"end":{"value":146,"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":193,"modifier":"EXACT"},"end":{"value":194,"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":225,"modifier":"EXACT"},"end":{"value":225,"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":247,"modifier":"EXACT"},"end":{"value":249,"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":326,"modifier":"EXACT"},"end":{"value":326,"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":"Disulfide bond","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"(transient)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"26383649","citationType":"journal article","authors":["Sprague L.D.","Neubauer H."],"citationCrossReferences":[{"database":"PubMed","id":"26383649"}],"title":"De Novo Genome Sequence of Yersinia aleksiciae Y159T.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"e01066","lastPage":"e01015","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32722.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}],"value":"159","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKP32722.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000069914"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP011975","properties":[{"key":"ProteinId","value":"AKP32722.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_048616943.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABMLM010000027.1"}]},{"database":"GeneID","id":"61904391","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"yak:ACZ76_03750","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000069914","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.530:FF:000001","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000008","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"NF008396","properties":[{"key":"EntryName","value":"rlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEQLLTASTSIDVAPQPDNLVDATAPVTGKINLLDLNRQQMREFFAKMGEKPFRADQVMKWMYHYCYDDFEQMTDINKVLRAKLQRVAEIRAPEVAEEQRSTDGTIKWAIKVGDQQVETVYIPEADRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGSLKSTGTRPITNVVMMGMGEPLLNLNNVVPAMDIMMDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPTDDIRDEIVPINRKYNIETFLAAVRRYLDKSKANGGRVTVEYVMLDHINDSTEQAHQLAECLKDTPCKINLIPWNPFPGAPYGRSSNSRVDRFSKVLMDYGFTTIVRKTRGDDIDAACGQLAGDVIDRTKRTLKKKMAGEPIAIKTV","length":398,"molWeight":44330,"crc64":"BFFECA3995F28A66","md5":"AD3089282D56E0E358C5698C27147144"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7,"Disulfide bond":1},"uniParcId":"UPI0005DB8DB5"}}]}