{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6C4","uniProtkbId":"A0ACH1D6C4_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27047.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27047.1"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27047.1"}],"value":"PQQ29_08055"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27047.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27047.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27047.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003762450.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000001.1"}]},{"database":"SMR","id":"A0ACH1D6C4","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669408","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00763","properties":[{"key":"EntryName","value":"Bacterial_PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.450:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00339","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_B1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR012828","properties":[{"key":"EntryName","value":"PFKA_ATP_prok"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02482","properties":[{"key":"EntryName","value":"PFKA_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRIAILTSGGDAPGMNAATRAVVRKAIYEGLEVYGINYGFLGLVNGDIRKLELGSVGDLLHRGGTFLYSARYPEFATEEGQLKGIEQLKKHQIDGLVVIGGDGSYHGAEALTKRGFPTIGIPGTIDNDISGTDFTIGFDTALNTVLDALDKIRDTATSHERTFIIEVMGRDAGDIALWSGLAGGAEAIIVPEESFNMDDVVDRLNKGRERGKKHSIIVVAEGVMSGNEFAKQLAEYGDYHARVTVLGHVQRGGSPTAFDRVLASRLGARSVELLLENRGGLAVGIRENRIVENNIGEILKEKHTLDQKLFDLASILSI","length":319,"molWeight":34389,"crc64":"10B57F77691BBD95","md5":"0C4945042DF9CE39F8B3C314632515CD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":15},"uniParcId":"UPI000012DB57"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6W8","uniProtkbId":"A0ACH1D6W8_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27312.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"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":"WCT27312.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27312.1"}],"value":"PQQ29_09550"}]}],"comments":[{"texts":[{"evidences":[{"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060037"}],"value":"Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of the biosynthetic pathway leading 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":"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":"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":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":861,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":930,"modifier":"EXACT"},"end":{"value":1070,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":547,"modifier":"EXACT"},"end":{"value":929,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":930,"modifier":"EXACT"},"end":{"value":1070,"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":284,"modifier":"EXACT"},"end":{"value":284,"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":284,"modifier":"EXACT"},"end":{"value":284,"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":284,"modifier":"EXACT"},"end":{"value":284,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":300,"modifier":"EXACT"},"end":{"value":300,"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":300,"modifier":"EXACT"},"end":{"value":300,"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":707,"modifier":"EXACT"},"end":{"value":707,"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":746,"modifier":"EXACT"},"end":{"value":746,"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":748,"modifier":"EXACT"},"end":{"value":748,"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":752,"modifier":"EXACT"},"end":{"value":752,"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":777,"modifier":"EXACT"},"end":{"value":777,"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":778,"modifier":"EXACT"},"end":{"value":778,"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":779,"modifier":"EXACT"},"end":{"value":779,"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":780,"modifier":"EXACT"},"end":{"value":780,"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":820,"modifier":"EXACT"},"end":{"value":820,"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":820,"modifier":"EXACT"},"end":{"value":820,"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":820,"modifier":"EXACT"},"end":{"value":820,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":834,"modifier":"EXACT"},"end":{"value":834,"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":834,"modifier":"EXACT"},"end":{"value":834,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27312.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27312.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27312.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010991677.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"SMR","id":"A0ACH1D6W8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669780","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000026","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000011","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":"2"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_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":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"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"}]}],"sequence":{"value":"MPKRDDIKTILVIGSGPIVIGQAAEFDYAGTQACLSLKEEGYRVVLVNSNPATIMTDAEMADKVYIEPITLDFVSRIIRKERPDAILPTLGGQTGLNMAMELSAAGILDECNVEVLGTDLTAIKKAEDREAFRDLMNELGEPVPESDIIHNLDEAYTFVERIGYPVIVRPAYTLGGSGGGICHNEQELIETVTSGLKLSPVTQCLLEKSIAGFKEVEYEVMRDANNNAMVVCNMENIDPVGIHTGDSIVVAPSQTLSDREYQLLRDVSLKIIRALEIEGGCNVQLALDPDSYNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEVRNPVTGTTYAHFEPTLDYVVAKIPRFAFDKFEQADRRLGTQMKATGEVMAIGRSWEEALLKAVRSLEIGADHLLLEEAENADAETLERKICFPEDDRLFFLAAALRRGQTIEQLHAKTKIDLFFLYKLSKTIELENRLKENPQNEEILAEAKRAGFSDAFIATCWNIDEQAIYDLRKAQNLFPVYKMVDTCAAEFESTTPYFYSTYEDENESIRSSKESVIVLGSGPIRIGQGVEFDYATVHSVWAIQQAGYEAIIINNNPETVSTDFSISDKLYFEPLTLEDVMHVIEIEQPLGVVVQFGGQTAINLADGLAKRGVKILGTSLEDTDRAENRDAFEKALEILQIPQPAGKTATSVEAAIKVATDIGYPVLVRPSYVLGGRAMEIVESEEALKHYMTNAVKVNPKHPVLVDRYVSGQEVEVDAISDGENVLIPGIMEHIERAGVHSGDSIAVYPAQRLSEQVKNTIVDYTTRLATGLNIIGMLNIQYVVDGEEVFVIEVNPRSSRTAPFLSKITEIPMANVATRVILGENLIDLGYTPGLAPEKQEIFVKVPVFSFAKLRSVDTSLGPEMKSTGEVMGKDVTLEKALYKGFVASGTTMHDYGTVLLTVADRDKEEAVELAKRFNRIGFTIMATKGTASTLEEAEIPVSQVKKIGENQETLIDYIRNGQVTLVVNTLTTGKRPERDGFQIRRESVENGIPVCTSLDTAEAILRVLESRSFELESMNASEVKQPKARV","length":1070,"molWeight":117861,"crc64":"9783DC3C9D8EF197","md5":"273BE842B4A34BCE0A21529E078D6A6C"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":3,"Binding site":38},"uniParcId":"UPI0000126F84"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D7K8","uniProtkbId":"A0ACH1D7K8_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27303.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27303.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27303.1"}],"value":"PQQ29_09500"}]}],"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":2,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"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":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27303.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27303.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27303.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_187983947.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"GeneID","id":"93235277","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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":"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":"MQGKNILLAVSGGIAVYKAVALTSKLTQAGANVKVMMTEHAQEFVPPLSFQVLSKNDVYTDTFDEKKSSVVAHIDLADWADLVIVAPATANLIGKMANGIADDMVTTTILATEAPVWVAPAMNVHMIQHPAVIRNINRLYADGVRFIEPEEGYLACGYVGRGRLEEPEKIVLRIAEFFQEDKDLLQGKKVLVTAGATREKLDPVRYFTNHSTGKMGFSIAESAARHGANVTLITTSKTLPVPPGVEAVYVESADEMYQAVLERKAEQHIFVMTAAVADYTPANVSEQKIKKQPGDFTIEMKRTKDILLEIGQNKTADQVVIGFAAETENLETNALKKLTSKNADMIVANNISEAGAGFSGDTNIVTFYRKDGSNEALPLLDKKEVAEHIIEEAANFLRK","length":399,"molWeight":43510,"crc64":"21E4380F3958B1F5","md5":"5775FEFE59D39B51D95F317ECB263A66"},"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":5},"uniParcId":"UPI001077917C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D8X0","uniProtkbId":"A0ACH1D8X0_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27565.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27565.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27565.1"}],"value":"PQQ29_10845"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}]},{"type":"Active site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27565.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27565.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27565.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003769677.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000002.1"}]},{"database":"GeneID","id":"93235546","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKIGVLALQGAVDEHIQMIESAGALAFKVKHSNDLAGLDGLVLPGGESTTMRKIMKRYDLMEPVKAFAKEGKAIFGTCAGLVLLSKEIEGGEESLGLLDATAIRNGFGRQKESFEAELTVEVFDDSPFEAVFIRAPYLIEPSDEVSVLATVENRIVAAKQANILVTAFHPELTNDNRLMKYFLEKMV","length":188,"molWeight":20547,"crc64":"2605FF569246790C","md5":"E9C8F61F9B8430CDD38782DCD55D048C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI00024556E8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D9B0","uniProtkbId":"A0ACH1D9B0_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27941.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27941.1"}],"value":"PQQ29_12955"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":507,"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":509,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"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":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"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":148,"modifier":"EXACT"},"end":{"value":150,"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":188,"modifier":"EXACT"},"end":{"value":193,"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":188,"modifier":"EXACT"},"end":{"value":193,"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":224,"modifier":"EXACT"},"end":{"value":224,"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":224,"modifier":"EXACT"},"end":{"value":224,"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":354,"modifier":"EXACT"},"end":{"value":354,"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":382,"modifier":"EXACT"},"end":{"value":385,"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":405,"modifier":"EXACT"},"end":{"value":405,"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":462,"modifier":"EXACT"},"end":{"value":462,"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":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27941.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27941.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27941.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010991341.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAFVD010000048.1"}]},{"database":"SMR","id":"A0ACH1D9B0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51670564","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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":"MTKYIFVTGGVVSSIGKGITAASLGRLLKNRGLSVTIQKFDPYINVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKVYSEVIKKERRGDYLGGTVQVIPHITNELKDRVFRAARMTNSDIIITEIGGTVGDIESLPFLEAIRQIKSDVGAENVLYIHTTLIPYIKAAGEMKTKPTQHSVKELRSLGIQPNIIVVRTEQPVSQEMKDKIALFCDIKASEVIESRDEETLYNVPLSLQKQKMDDIVLEHLQLEAPQAEMTDWKNLVHRVKNLSKKVRIGLVGKYVSLQDAYLSVAEALRHAGYEHDAEIEIDWIDSEKVTKENVAEIMKDVDGILVPGGFGDRAIEGKIAAIEYARVNKVPYFGICLGMQLATVEFARNVLGLEGAHSAEIEPETKHNIIDLLPEQKNIENMGGTLRLGLYPARIKQGTKAEAAYGTTLVEERHRHRYEFNNEYREQMEEAGMIVSATSPDGRLVEVVELADHPWFVACQYHPEFISRPNRPQSLFKDFVGAALNNK","length":532,"molWeight":59569,"crc64":"20589487015CBA96","md5":"F5DFBEFC303106A04684355F4FFB4E41"},"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":"UPI0000132D66"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D9C5","uniProtkbId":"A0ACH1D9C5_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27503.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"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"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27503.1"}],"value":"PQQ29_10530"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056782"},{"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":"ARBA","id":"ARBA00004752"},{"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":23,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"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":108,"modifier":"EXACT"},"end":{"value":114,"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":149,"modifier":"EXACT"},"end":{"value":149,"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":150,"modifier":"EXACT"},"end":{"value":151,"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":177,"modifier":"EXACT"},"end":{"value":177,"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":183,"modifier":"EXACT"},"end":{"value":183,"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":383,"modifier":"EXACT"},"end":{"value":383,"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":407,"modifier":"EXACT"},"end":{"value":410,"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":458,"modifier":"EXACT"},"end":{"value":458,"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":462,"modifier":"EXACT"},"end":{"value":462,"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":217,"modifier":"EXACT"},"end":{"value":217,"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":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27503.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27503.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27503.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010991030.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"SMR","id":"A0ACH1D9C5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669974","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0004326","properties":[{"key":"GoTerm","value":"F:tetrahydrofolylpolyglutamate synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"3.40.1390.10:FF:000005","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":"IPR018109","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth_CS"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01011","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLKELMQAIPVYTGEASAAIEVNQIAQDSRKVQPGTLFICIDGEIVDGHQFADRAVQLGAVAIIAEKQLDVSVPVLYVRDSKRAMAMLADYFYGSPTQALKLVGITGTNGKTTVSHLVEQIVRENGEQTGLIGTMYRKIGDEILETKNTTPDSLTLQETFRDMLLSGVSTAVMEVSSHALVQGRVYGSDYDVAVFMNLSQDHLDYHHTMEEYAYAKSLLFAQLGNSYNLSNPKIAVLNADDKESVRMQTATAAHIITFGIKEPADFSASNIQITSHGSTFDLKTPVGDFALKIKMIGNFSVYNVLAAIATSFALRIPVINAIATVESIPGVKGRFELVNAGQDFPVIVDYSHTPDSLLNVLQTIDEFAEKRVFVVVGCGGDRDKGKRPQMAKIAVDYATNPIFTSDNPRSEDPHAIIEDMIQGVPGSDSYVVHENRRDAIRYAVNMAEAGDVILIAGKGHEDYQVIGDEVIDFDDRVEARIAIEKKLGLA","length":491,"molWeight":53612,"crc64":"FDC0EC28825F6005","md5":"5C39801465146A1C6C093EFE9A7D4DD2"},"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":11,"Modified residue":1},"uniParcId":"UPI000012F99F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1DAH7","uniProtkbId":"A0ACH1DAH7_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28391.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"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":"WCT28391.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28391.1"}],"value":"PQQ29_01475"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005166"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005208"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":457,"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":9,"modifier":"EXACT"},"end":{"value":12,"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":23,"modifier":"EXACT"},"end":{"value":23,"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":73,"modifier":"EXACT"},"end":{"value":73,"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":78,"modifier":"EXACT"},"end":{"value":79,"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":103,"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":155,"modifier":"EXACT"},"end":{"value":155,"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":170,"modifier":"EXACT"},"end":{"value":170,"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":228,"modifier":"EXACT"},"end":{"value":228,"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":228,"modifier":"EXACT"},"end":{"value":228,"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":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":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":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28391.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28391.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT28391.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010990291.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000003.1"}]},{"database":"SMR","id":"A0ACH1DAH7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51668029","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010934","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":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"3"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKRYAVVLAAGQGTRMKSKLYKVLHPVCGKPMVEHVVDQISTLDVDKVVTIVGHGAEKVQEHLAGKSEFVKQDEQLGTAHAVLQAKSELAGKDGVTLVVCGDTPLIEASTMEALLKYHHEKRAKATILTTVIEDPTGYGRIIRDDLGIVEKIVEHKDATEKEQRISEINTGTYCFDNKALFEALENVSNDNVQGEYYLPDVIKILKDADEVVAAYKMESFEESLGVNDRIALAEASKLMQRRINENHMRNGVTLVNPENTYIDIDVKIGQDTVIEPGVMLRGKTVIGDDCVVTSGSEIVSSVIGERVHVRNSSIFESKVGDDVQIGPYAHLRPESDIHNHVKIGNYVETKKAVVGEGTKLPHFIYMGDAEIGKNVNVGCGSIAVNYDGKNKAKTIIGDNVFVGCNSNLIAPVKVGDRAFIAAGSTITKDVPEDALGIARAKQDNKLGYAKHLNHGK","length":457,"molWeight":49766,"crc64":"2C031A52945ECAA7","md5":"8A06FE6C8E04E845E3727C83AE4DFA23"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":17},"uniParcId":"UPI00000CC17F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1DB98","uniProtkbId":"A0ACH1DB98_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28405.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"tRNA(Ile)-lysidine synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"6.3.4.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"tRNA(Ile)-2-lysyl-cytidine synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"tRNA(Ile)-lysidine synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"tilS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28405.1"}],"value":"PQQ29_01545"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057249"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25424"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58115"}],"ecNumber":"2.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051961"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17973"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58053"}],"ecNumber":"2.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051203"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine(34) in tRNA(Ile2) + L-lysine + ATP = lysidine(34) in tRNA(Ile2) + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43744"},{"database":"Rhea","id":"RHEA-COMP:10625"},{"database":"Rhea","id":"RHEA-COMP:10670"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32551"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:82748"},{"database":"ChEBI","id":"CHEBI:83665"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.4.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048539"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"value":"Belongs to the tRNA(Ile)-lysidine synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010138"}],"value":"In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061707"}],"value":"In the N-terminal section; belongs to the tRNA(Ile)-lysidine synthase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Lysidine-tRNA(Ile) synthetase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00977"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28405.1"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01161"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28405.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28405.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT28405.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010990297.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"SMR","id":"A0ACH1DB98","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51670938","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0052657","properties":[{"key":"GoTerm","value":"F:guanine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004422","properties":[{"key":"GoTerm","value":"F:hypoxanthine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0032267","properties":[{"key":"GoTerm","value":"F:tRNA(Ile)-lysidine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006177","properties":[{"key":"GoTerm","value":"P:GMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006188","properties":[{"key":"GoTerm","value":"P:IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006166","properties":[{"key":"GoTerm","value":"P:purine ribonucleoside salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006400","properties":[{"key":"GoTerm","value":"P:tRNA modification"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01992","properties":[{"key":"EntryName","value":"TilS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000006","properties":[{"key":"EntryName","value":"Hypoxanthine phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.465.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","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_01161","properties":[{"key":"EntryName","value":"tRNA_Ile_lys_synt"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005904","properties":[{"key":"EntryName","value":"Hxn_phspho_trans"}]},{"database":"InterPro","id":"IPR012796","properties":[{"key":"EntryName","value":"Lysidine-tRNA-synth_C"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR011063","properties":[{"key":"EntryName","value":"TilS/TtcA_N"}]},{"database":"InterPro","id":"IPR012094","properties":[{"key":"EntryName","value":"tRNA_Ile_lys_synt"}]},{"database":"InterPro","id":"IPR012795","properties":[{"key":"EntryName","value":"tRNA_Ile_lys_synt_N"}]},{"database":"NCBIfam","id":"TIGR01203","properties":[{"key":"EntryName","value":"HGPRTase"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02433","properties":[{"key":"EntryName","value":"lysidine_TilS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02432","properties":[{"key":"EntryName","value":"lysidine_TilS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43033","properties":[{"key":"EntryName","value":"TRNA(ILE)-LYSIDINE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43033:SF1","properties":[{"key":"EntryName","value":"TRNA(ILE)-LYSIDINE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01171","properties":[{"key":"EntryName","value":"ATP_bind_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11734","properties":[{"key":"EntryName","value":"TilS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00977","properties":[{"key":"EntryName","value":"TilS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF82829","properties":[{"key":"EntryName","value":"MesJ substrate recognition domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56037","properties":[{"key":"EntryName","value":"PheT/TilS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDDTKKRIHKYIEKHDLIRSDDKLLVAVSGGPDSFALLHFLWSANLVPKEAIAVAHLNHHLRENAEKEQLAVQTFCEERDIPFFIEEVDVKKRAEKLQKGIEETARIVRYDFFEKVMAENNINKLVLAHHADDQIETILMRLVRGSSSIGWSGIQPKREVRGGYAIRPFLPITKAEIIEYATKHALPYEIDESNTSQEYTRNRYRTQLLPFLSKENPAVYEHFKRFSEETSEDFQFLEELASNLLKKNLIQNGKQSTLLLSDFKNEANPLQRRAIHLLLMYLYNDDGRVITVNHIYQIIQMIQSENPSSSIDLPKKLTVIRSYNELHFQFGERHAPPEFYHQLELNDRIELDNKASIRLKLKSSVVQTNGLNGMLLDAEDITLPLIVRNRVNGDRMTMKGQAGSKKLKDIFIDAKIPRQERDNLPVITDYTGKILWVPGVKKSAYDREFSRSKKQYIIRYTRNIGGNESMHNDIQKVLISEDELQEKIRELGRELTAEYEGRNPLVVGVLKGATPFMTDLLKRIDTYLEMDFMDVSSYGNGTVSSGEVKIIKDLNASVEGRDVLIIEDIIDSGRTLSYLVDLIKYRKAKSVKLVTLLDKPAGRNVAIEADYVGFVVPNEFVVGYGLDYAERYRNLPYIGILKPEIYSE","length":648,"molWeight":74527,"crc64":"796860D8E403E0CD","md5":"B8723BF91F202957FA5E2B3FCCB57555"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":3},"countByFeatureType":{"Domain":1,"Binding site":1},"uniParcId":"UPI00000CC185"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1DBH6","uniProtkbId":"A0ACH1DBH6_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28625.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28625.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28625.1"}],"value":"PQQ29_02775"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"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":116,"modifier":"EXACT"},"end":{"value":116,"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":119,"modifier":"EXACT"},"end":{"value":119,"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":164,"modifier":"EXACT"},"end":{"value":165,"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":196,"modifier":"EXACT"},"end":{"value":196,"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":219,"modifier":"EXACT"},"end":{"value":221,"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":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28625.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT28625.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT28625.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003725208.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CBCPHM010000001.1"}]},{"database":"SMR","id":"A0ACH1DBH6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51668289","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKSSIYGLTWTKLTEWLEAHGQKKFRATQVWDWLYRKRVKTFEEMSNVPKETIELLTANFVMNTLEEQVVQESTDGTTKYLFKLSDGNLIETVMMKQEYGLSVCVTTQVGCNIGCTFCASGLLKKSRDLTAGEIVEQIMNVQHYLDGRNLEERVSHVVVMGIGEPFDNYDNVMDFLRVINHDKGLAIGARHITVSTSGLAPRIIDFANEDFQVNLAISLHAPNNELRTSIMRINKTYSIEKLMEAIHYYVNKTNRRITFEYIMLKGVNDHKKEALELAALLGEHRHLAYVNLIPYNPVDEHIDYERSTKEDVLAFYDTLKKNGINCVIRREHGTDIDAACGQLRSKQIKRVGVRERMKQKQAAAEE","length":367,"molWeight":42101,"crc64":"51F60BE6DB31A165","md5":"CE0EE33B284D0354CA0DD1981637D3BB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI00000CC251"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6Q3I1","uniProtkbId":"Q6Q3I1_LISIO","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":80,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAS67617.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074764"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000111"}],"value":"Aldehyde-alcohol dehydrogenase"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAS67617.1"}],"value":"aad"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an aldehyde + NAD(+) + H2O = a carboxylate + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16185"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17478"},{"database":"ChEBI","id":"CHEBI:29067"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.2.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049194"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ethanol + NAD(+) = acetaldehyde + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25290"},{"database":"ChEBI","id":"CHEBI:15343"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16236"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052923"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001954"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007358"}],"value":"Belongs to the iron-containing alcohol dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00035645"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000111"}],"value":"In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00035641"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000111"}],"value":"In the N-terminal section; belongs to the aldehyde dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Aldehyde dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00171"}]},{"type":"Domain","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00465"}]},{"type":"Domain","location":{"start":{"value":653,"modifier":"EXACT"},"end":{"value":863,"modifier":"EXACT"}},"description":"Fe-containing alcohol dehydrogenase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF25137"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"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":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000111"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9NV494ULF8JPL","citationType":"submission","authors":["Kim K.-P.","Bhunia A.K."],"title":"The heterogeneity of alcohol acetaldehyde dehydrogenase in different Listeria species.","publicationDate":"FEB-2004","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAS67617.1"}],"value":"F4248","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAS67617.1"}]},{"referenceNumber":2,"citation":{"id":"20507888","citationType":"journal article","authors":["Jagadeesan B.","Koo O.K.","Kim K.P.","Burkholder K.M.","Mishra K.K.","Aroonnual A.","Bhunia A.K."],"citationCrossReferences":[{"database":"PubMed","id":"20507888"},{"database":"DOI","id":"10.1099/mic.0.036509-0"}],"title":"LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species.","publicationDate":"2010","journal":"Microbiology","firstPage":"2782","lastPage":"2795","volume":"156"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAS67617.1"}],"value":"F4248","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAS67617.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY561825","properties":[{"key":"ProteinId","value":"AAS67617.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6Q3I1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q6Q3I1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009986","properties":[{"key":"GoTerm","value":"C:cell surface"},{"key":"GoEvidenceType","value":"IDA:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20507888"}]},{"database":"GO","id":"GO:0009274","properties":[{"key":"GoTerm","value":"C:peptidoglycan-based cell wall"},{"key":"GoEvidenceType","value":"IDA:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20507888"}]},{"database":"GO","id":"GO:0008774","properties":[{"key":"GoTerm","value":"F:acetaldehyde dehydrogenase (acetylating) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004022","properties":[{"key":"GoTerm","value":"F:alcohol dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IDA:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20507888"}]},{"database":"GO","id":"GO:0004029","properties":[{"key":"GoTerm","value":"F:aldehyde dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0031072","properties":[{"key":"GoTerm","value":"F:heat shock protein binding"},{"key":"GoEvidenceType","value":"IPI:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"20507888"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046187","properties":[{"key":"GoTerm","value":"P:acetaldehyde catabolic process"},{"key":"GoEvidenceType","value":"IDA:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20507888"}]},{"database":"GO","id":"GO:0046164","properties":[{"key":"GoTerm","value":"P:alcohol catabolic process"},{"key":"GoEvidenceType","value":"IDA:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20507888"}]},{"database":"GO","id":"GO:0015976","properties":[{"key":"GoTerm","value":"P:carbon utilization"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd08178","properties":[{"key":"EntryName","value":"AAD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07122","properties":[{"key":"EntryName","value":"ALDH_F20_ACDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1090.10:FF:000001","properties":[{"key":"EntryName","value":"Aldehyde-alcohol dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.309.10:FF:000007","properties":[{"key":"EntryName","value":"Aldehyde-alcohol dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000002","properties":[{"key":"EntryName","value":"Aldehyde-alcohol dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.605.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.309.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR034789","properties":[{"key":"EntryName","value":"AAD_C"}]},{"database":"InterPro","id":"IPR001670","properties":[{"key":"EntryName","value":"ADH_Fe/GldA"}]},{"database":"InterPro","id":"IPR056798","properties":[{"key":"EntryName","value":"ADH_Fe_C"}]},{"database":"InterPro","id":"IPR018211","properties":[{"key":"EntryName","value":"ADH_Fe_CS"}]},{"database":"InterPro","id":"IPR039697","properties":[{"key":"EntryName","value":"Alcohol_dehydrogenase_Fe"}]},{"database":"InterPro","id":"IPR016161","properties":[{"key":"EntryName","value":"Ald_DH/histidinol_DH"}]},{"database":"InterPro","id":"IPR016163","properties":[{"key":"EntryName","value":"Ald_DH_C"}]},{"database":"InterPro","id":"IPR016162","properties":[{"key":"EntryName","value":"Ald_DH_N"}]},{"database":"InterPro","id":"IPR015590","properties":[{"key":"EntryName","value":"Aldehyde_DH_dom"}]},{"database":"InterPro","id":"IPR012079","properties":[{"key":"EntryName","value":"Bifunc_Ald-ADH"}]},{"database":"NCBIfam","id":"NF010378","properties":[{"key":"EntryName","value":"adhE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11496","properties":[{"key":"EntryName","value":"ALCOHOL DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11496:SF83","properties":[{"key":"EntryName","value":"HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25137","properties":[{"key":"EntryName","value":"ADH_Fe_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00171","properties":[{"key":"EntryName","value":"Aldedh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00465","properties":[{"key":"EntryName","value":"Fe-ADH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000111","properties":[{"key":"EntryName","value":"ALDH_ADH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53720","properties":[{"key":"EntryName","value":"ALDH-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00913","properties":[{"key":"EntryName","value":"ADH_IRON_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAIKENAAQEVLEVQKVIDRLADNGQKALKAFESYNQEQVDNIVHAMALAGLDQHMPLAKLAVEETGRGLYEDKCIKNIFATEYIWNNIKNNKTVGVINEDTQTGVIEIAEPVGVVAGVTPVTNPTSTTLFKAIIAIKTRNPIIFAFHPSAQRCSSEAAKVVYDAAVAAGAPEHCIQWVEKPSLEATKQLMNHDKVALVLATGGAGMVKSAYSTGKPALGVGPGNVPAYIDKTAKIKRSVNDIILSKSFDQGMICASEQAVIVDKEVAKEVKAEMEANKCYFVKGAEFKKLESYVINPEKGTLNPDVVGKSPAWIANQAGFKVPEDTKILVAEIKGVGDKYPLSHEKLSPVLAFIEAATQAEAFDRCEEMLVYGGLGHSAVIHSTDKEVQKAFGIRMKACRIIVNAPSAQGGIGDIYNGFIPSLTLGCGSYGKNSVSQNVSATNLLNVKRIADRRNNMQWFKLPPKIFFEKYSTQYLQKMEGVERVFIVTDPGMVQFKYVDVVIEHLKKRGNDVAYQVFADVEPDPSDVTVYKGAELMKDFKPDTIIALGGGSAMDAAKGMWLFYEHPEASFFGLKQKFLDIRKRTFKYPKLGGKAKFVAIPTTSGTGSEVTPFAVITDKENNIKYPLADYELTPDVAIVDAQYVTTVPAHITADTGMDVLTHAIESYVSVMASDYTRGLSIRAIELVFENLRESVLTGDPDAREKMHNASALAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVIRYNALKPKKHALFPRYESFRADEDYARISRIIGFPAATTEEGVKSLVDEIIKLGKDVGIDMSLKGQNVAKKDLDAVVDTLADRAFMDQCTTANPKQPLVSELKEIYLEAYKGV","length":866,"molWeight":94699,"crc64":"7F465A7038535A85","md5":"AA3B8568B861F93D3D377677A7A0A11C"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SIMILARITY":3},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0000350282"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A146FAY1","uniProtkbId":"A0A146FAY1_LISIO","entryAudit":{"firstPublicDate":"2016-06-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-06-08","entryVersion":36,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAU68518.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012729"}],"value":"chitinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012729"}],"value":"3.2.1.14"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAU68518.1"}],"value":"lin0153"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.","ecNumber":"3.2.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000822"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"value":"Belongs to the glycosyl hydrolase 18 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":756,"modifier":"EXACT"}},"description":"chitinase","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5052417994"},{"type":"Domain","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"GH18","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51910"}]},{"type":"Domain","location":{"start":{"value":620,"modifier":"EXACT"},"end":{"value":705,"modifier":"EXACT"}},"description":"Fibronectin type-III","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50853"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}]},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17029"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"ligand":{"name":"chitin","id":"ChEBI:CHEBI:17029"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17029"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"ligand":{"name":"chitin","id":"ChEBI:CHEBI:17029"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17029"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"ligand":{"name":"chitin","id":"ChEBI:CHEBI:17029"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17029"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"ligand":{"name":"chitin","id":"ChEBI:CHEBI:17029"}},{"type":"Binding site","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17029"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"ligand":{"name":"chitin","id":"ChEBI:CHEBI:17029"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023024"}],"id":"KW-0146","category":"Biological process","name":"Chitin degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023326"}],"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"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":"27138200","citationType":"journal article","authors":["Honda S.","Wakita S.","Sugahara Y.","Kawakita M.","Oyama F.","Sakaguchi M."],"citationCrossReferences":[{"database":"PubMed","id":"27138200"},{"database":"DOI","id":"10.1007/s00253-016-7546-0"}],"title":"Characterization of two Listeria innocua chitinases of different sizes that were expressed in Escherichia coli.","publicationDate":"2016","journal":"Appl. Microbiol. Biotechnol.","firstPage":"8031","lastPage":"8041","volume":"100"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAU68518.1"}],"value":"Clip11262","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAU68518.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LC092875","properties":[{"key":"ProteinId","value":"BAU68518.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010990239.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"AlphaFoldDB","id":"A0A146FAY1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A146FAY1","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51667946","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.2.1.14","properties":[{"key":"OrganismId","value":"3044"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008061","properties":[{"key":"GoTerm","value":"F:chitin binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008843","properties":[{"key":"GoTerm","value":"F:endochitinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd12215","properties":[{"key":"EntryName","value":"ChiC_BD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00063","properties":[{"key":"EntryName","value":"FN3"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd06548","properties":[{"key":"EntryName","value":"GH18_chitinase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd20174","properties":[{"key":"EntryName","value":"GH18_LinChi78-like_UFR"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.10:FF:001114","properties":[{"key":"EntryName","value":"Chitinase A1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.50.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.10.10.20","properties":[{"key":"EntryName","value":"Carbohydrate-binding module superfamily 5/12"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003610","properties":[{"key":"EntryName","value":"CBM5/12"}]},{"database":"InterPro","id":"IPR036573","properties":[{"key":"EntryName","value":"CBM_sf_5/12"}]},{"database":"InterPro","id":"IPR011583","properties":[{"key":"EntryName","value":"Chitinase_II/V-like_cat"}]},{"database":"InterPro","id":"IPR029070","properties":[{"key":"EntryName","value":"Chitinase_insertion_sf"}]},{"database":"InterPro","id":"IPR003961","properties":[{"key":"EntryName","value":"FN3_dom"}]},{"database":"InterPro","id":"IPR036116","properties":[{"key":"EntryName","value":"FN3_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR001223","properties":[{"key":"EntryName","value":"Glyco_hydro18_cat"}]},{"database":"InterPro","id":"IPR050314","properties":[{"key":"EntryName","value":"Glycosyl_Hydrlase_18"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"PANTHER","id":"PTHR11177","properties":[{"key":"EntryName","value":"CHITINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11177:SF317","properties":[{"key":"EntryName","value":"CHITINASE 12-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02839","properties":[{"key":"EntryName","value":"CBM_5_12"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00041","properties":[{"key":"EntryName","value":"fn3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00704","properties":[{"key":"EntryName","value":"Glyco_hydro_18"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00495","properties":[{"key":"EntryName","value":"ChtBD3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00060","properties":[{"key":"EntryName","value":"FN3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00636","properties":[{"key":"EntryName","value":"Glyco_18"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51055","properties":[{"key":"EntryName","value":"Carbohydrate binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54556","properties":[{"key":"EntryName","value":"Chitinase insertion domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49265","properties":[{"key":"EntryName","value":"Fibronectin type III"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50853","properties":[{"key":"EntryName","value":"FN3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51910","properties":[{"key":"EntryName","value":"GH18_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKLFSITSVVLLVLSLVVVSIGAESKRAKAAENVPQYRNVMYYGDWSIWGGEGNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGAPVGQEGVQWGGANAGVLNAIQDLRAQNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASVRDADLVDNKNDEGTPNAKPADKQNFITLLQDLRTALDKQGVDINKKYELSVALPAAKSTLENGVDVANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGNPKDPNYNSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDTALPGLFQAAEKTNKDADGSLTYGANNENPIKTGDGGRAGGVWAYRSIDALKAKTPTLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQDKTTTSTKRDELTKAIKTGLFGTSAIPQNAITYANLNVVATVKPYSENGVGYEITITNNEKADETNEVLKSTELSFETVKLPKFYIPVKAGETLTAGDYKAGTVTTSGGNTVVDLASVYDAQQIPQGASYTFRLKSSASSVDVNNISKIDLTQRMVKSSVEFGKQTIFGGGTVVPDPSDTEAPTVPKSLASSNVTDKSVTLSWTASTDNKAVAGYKVYRNGTEVGSVSGTTFTDSGLTAKTAYTYTVKAYDAAGNFSAASSALTVTTLDAATPPATPAWDAAKTYNKGDRVSYKGKTYEAQWWTQGNEPGAEQWGPWLLIN","length":756,"molWeight":81574,"crc64":"39CDB1C5399BB50F","md5":"42A696D5EAFB07274F82921550300110"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":2,"Active site":1,"Binding site":5},"uniParcId":"UPI00000CC134"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D5Z9","uniProtkbId":"A0ACH1D5Z9_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012891"}],"value":"DNA topoisomerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012891"}],"value":"5.6.2.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032877"}],"value":"Omega-protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032235"}],"value":"Relaxing enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030003"}],"value":"Swivelase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031985"}],"value":"Untwisting enzyme"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"}],"value":"topB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"}],"value":"PQQ29_00510"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.","ecNumber":"5.6.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000213"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10131"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009446"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01383"}],"value":"Belongs to the type IA topoisomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Toprim","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50880"}]},{"type":"Domain","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":600,"modifier":"EXACT"}},"description":"Topo IA-type catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS52039"}]},{"type":"Active site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10131"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"value":"pATCC33090_1","geneEncodingType":"Plasmid"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01383"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01383"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"}],"id":"KW-0614","category":"Technical term","name":"Plasmid"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023029"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01383"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"}],"value":"ATCC 33090","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"}],"value":"pATCC33090_1","type":"PLASMID"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26877.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117228","properties":[{"key":"ProteinId","value":"WCT26877.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_077316122.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP102628.1"}]},{"database":"GeneID","id":"93233480","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","properties":[{"key":"Component","value":"Plasmid pATCC33090_1"}]},{"database":"GO","id":"GO:0043597","properties":[{"key":"GoTerm","value":"C:cytoplasmic replication fork"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003917","properties":[{"key":"GoTerm","value":"F:DNA topoisomerase type I (single strand cut, ATP-independent) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00186","properties":[{"key":"EntryName","value":"TOP1Ac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03362","properties":[{"key":"EntryName","value":"TOPRIM_TopoIA_TopoIII"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.460.10","properties":[{"key":"EntryName","value":"Topoisomerase I, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.20.10","properties":[{"key":"EntryName","value":"Topoisomerase I, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.290.10","properties":[{"key":"EntryName","value":"Topoisomerase I, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000380","properties":[{"key":"EntryName","value":"Topo_IA"}]},{"database":"InterPro","id":"IPR003601","properties":[{"key":"EntryName","value":"Topo_IA_2"}]},{"database":"InterPro","id":"IPR023406","properties":[{"key":"EntryName","value":"Topo_IA_AS"}]},{"database":"InterPro","id":"IPR013497","properties":[{"key":"EntryName","value":"Topo_IA_cen"}]},{"database":"InterPro","id":"IPR013824","properties":[{"key":"EntryName","value":"Topo_IA_cen_sub1"}]},{"database":"InterPro","id":"IPR013825","properties":[{"key":"EntryName","value":"Topo_IA_cen_sub2"}]},{"database":"InterPro","id":"IPR013826","properties":[{"key":"EntryName","value":"Topo_IA_cen_sub3"}]},{"database":"InterPro","id":"IPR023405","properties":[{"key":"EntryName","value":"Topo_IA_core_domain"}]},{"database":"InterPro","id":"IPR003602","properties":[{"key":"EntryName","value":"Topo_IA_DNA-bd_dom"}]},{"database":"InterPro","id":"IPR005738","properties":[{"key":"EntryName","value":"TopoIII"}]},{"database":"InterPro","id":"IPR025589","properties":[{"key":"EntryName","value":"Toprim_C_rpt"}]},{"database":"InterPro","id":"IPR006171","properties":[{"key":"EntryName","value":"TOPRIM_dom"}]},{"database":"InterPro","id":"IPR034144","properties":[{"key":"EntryName","value":"TOPRIM_TopoIII"}]},{"database":"NCBIfam","id":"TIGR01056","properties":[{"key":"EntryName","value":"topB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11390:SF21","properties":[{"key":"EntryName","value":"DNA TOPOISOMERASE 3-ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11390","properties":[{"key":"EntryName","value":"PROKARYOTIC DNA TOPOISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01131","properties":[{"key":"EntryName","value":"Topoisom_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01751","properties":[{"key":"EntryName","value":"Toprim"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13342","properties":[{"key":"EntryName","value":"Toprim_Crpt"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00417","properties":[{"key":"EntryName","value":"PRTPISMRASEI"}]},{"database":"SMART","id":"SM00437","properties":[{"key":"EntryName","value":"TOP1Ac"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00436","properties":[{"key":"EntryName","value":"TOP1Bc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00493","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56712","properties":[{"key":"EntryName","value":"Prokaryotic type I DNA topoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00396","properties":[{"key":"EntryName","value":"TOPO_IA_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS52039","properties":[{"key":"EntryName","value":"TOPO_IA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50880","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKTVILAEKPSQAKEYASAMEMHSIKKGYIEIKDKLFPEGAIVTYGFGHLVELCLPGDYGEEYNKWSLANLPIFPEMKYRVAKDKIEQFSIVKGHLQKATQIIIATDCDREGELIAWLIINQAGINRNEKKVDRLWINSLEKEAIRKGFKSLRSSDETYDKFLEAQTRQKSDWLVGMNLSPLYTLSLQEKGVQGVFPIGRVQTPTLMMIYKRQKEIESFISKKYYEIELKGNQNKLLWTARLKEKQKFDSKESCKTFLENEKLKEGKQNVLVTNIQKEMKETQSPRLFSLSALQVVMSKKEKVSPKKVLESVQKLYEKKLLTYPRTDSVYITENELEYLLSLKESYQKLFSINQHLDHVDKKTRFVNSKKVHEHHAIIPTKKIPSQTELQGLTDLERNIYELVTRTTLAMFAETYQYEETTVDLLSNNVPFAAKGKVEKLLGWKSILNDVVEKEPDESTIPSLELDMFIEMDLQVISKDTKPQKAFTEGALIQAMKTAGKELENEEAQSILKDVEGIGTEATRADVIEKLKSQDYINVVKNQLEVTKKGQQIGKVLESDKLFSSAEMTALWEKDLKSISEDALTQDVFLKRIKHLVKSYIKQVPQNLDNISKETEWQEMQKVQSVGVCPNCGKDIVDRGKMYSCVGYKDKSSCSFTLMKKIMGKTLPQKDVSLLLSDGSTRTIKGFVSKKGNKFDAQLKWDKDKITFVFPNKK","length":713,"molWeight":81822,"crc64":"A413B0285035656D","md5":"F383DB557F5370757DE58B848E00372B"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1},"uniParcId":"UPI000986E51A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D657","uniProtkbId":"A0ACH1D657_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066744"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Elongation factor 4"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"EF-4"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066744"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"3.6.5.n1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Ribosomal back-translocase LepA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26957.1"}],"value":"lepA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26957.1"}],"value":"PQQ29_07590"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057626"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.n1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050293"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061052"}],"value":"Belongs to the GTP-binding elongation factor family. LepA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005454"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"value":"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26957.1"}],"id":"KW-0251","category":"Molecular function","name":"Elongation factor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00071"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26957.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26957.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT26957.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010991571.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"SMR","id":"A0ACH1D657","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669316","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043022","properties":[{"key":"GoTerm","value":"F:ribosome binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003746","properties":[{"key":"GoTerm","value":"F:translation elongation factor activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0045727","properties":[{"key":"GoTerm","value":"P:positive regulation of translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03699","properties":[{"key":"EntryName","value":"EF4_II"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd16260","properties":[{"key":"EntryName","value":"EF4_III"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01890","properties":[{"key":"EntryName","value":"LepA"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03709","properties":[{"key":"EntryName","value":"lepA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000078","properties":[{"key":"EntryName","value":"Elongation factor 4"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000015","properties":[{"key":"EntryName","value":"Translation factor GUF1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.240:FF:000007","properties":[{"key":"EntryName","value":"Translation factor GUF1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.2570:FF:000001","properties":[{"key":"EntryName","value":"Translation factor GUF1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.870:FF:000004","properties":[{"key":"EntryName","value":"Translation factor GUF1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.240","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.2570","properties":[{"key":"EntryName","value":"Elongation factor 4, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.870","properties":[{"key":"EntryName","value":"Elongation Factor G (Translational Gtpase), domain 3"},{"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":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00071","properties":[{"key":"EntryName","value":"LepA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006297","properties":[{"key":"EntryName","value":"EF-4"}]},{"database":"InterPro","id":"IPR035647","properties":[{"key":"EntryName","value":"EFG_III/V"}]},{"database":"InterPro","id":"IPR000640","properties":[{"key":"EntryName","value":"EFG_V-like"}]},{"database":"InterPro","id":"IPR004161","properties":[{"key":"EntryName","value":"EFTu-like_2"}]},{"database":"InterPro","id":"IPR031157","properties":[{"key":"EntryName","value":"G_TR_CS"}]},{"database":"InterPro","id":"IPR038363","properties":[{"key":"EntryName","value":"LepA_C_sf"}]},{"database":"InterPro","id":"IPR013842","properties":[{"key":"EntryName","value":"LepA_CTD"}]},{"database":"InterPro","id":"IPR035654","properties":[{"key":"EntryName","value":"LepA_IV"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005225","properties":[{"key":"EntryName","value":"Small_GTP-bd"}]},{"database":"InterPro","id":"IPR000795","properties":[{"key":"EntryName","value":"T_Tr_GTP-bd_dom"}]},{"database":"NCBIfam","id":"TIGR01393","properties":[{"key":"EntryName","value":"lepA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00231","properties":[{"key":"EntryName","value":"small_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43512:SF4","properties":[{"key":"EntryName","value":"TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43512","properties":[{"key":"EntryName","value":"TRANSLATION FACTOR GUF1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00679","properties":[{"key":"EntryName","value":"EFG_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00009","properties":[{"key":"EntryName","value":"GTP_EFTU"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03144","properties":[{"key":"EntryName","value":"GTP_EFTU_D2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06421","properties":[{"key":"EntryName","value":"LepA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00315","properties":[{"key":"EntryName","value":"ELONGATNFCT"}]},{"database":"SMART","id":"SM00838","properties":[{"key":"EntryName","value":"EFG_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54980","properties":[{"key":"EntryName","value":"EF-G C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00301","properties":[{"key":"EntryName","value":"G_TR_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51722","properties":[{"key":"EntryName","value":"G_TR_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNKEEMNARQKKIRNFSIIAHIDHGKSTLADRILEQTGALTHREMKNQLLDSMDLERERGITIKLNAVQLKYKAKDGETYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRAEIEDVIGLDASDTVLASAKSGIGIEDILEQIVEKVPEPSGDVDKPLKALIFDSVFDAYRGVIANIRIMDGVVKAGDRIKMMSNGKEFEVTEVGVFSPKATPRDELLVGDVGYLTAAIKNVGDTRVGDTITLANNPAEEALDGYRKLNPMVYCGLYPIDSSKYNDLRDALEKLELNDSALQFEAETSQALGFGFRCGFLGLLHMEIIQERIEREFNIDLITTAPSVIYHVNLTDGSNIVVDNPADMPEPGVIESVEEPYVKATVMVPNDYVGAVMELAQNKRGNFITMEYLDDIRVSIVYEIPLSEIVYDFFDQLKSSTKGYASFDYELIGYKASKLVKMDILLNAEKVDALSFIVHRDFAYERGKIIVEKLKELIPRQQFEVPIQAAIATKIVSRSTIKALRKNVLAKCYGGDVSRKRKLLEKQKEGKKRMKQIGSVEVPQEAFMAILKMDESK","length":608,"molWeight":67782,"crc64":"0F0FBC7C42EE87A6","md5":"A9A14C664DC924AB5831A3F1DD32CC6E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":2},"uniParcId":"UPI000012E479"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D658","uniProtkbId":"A0ACH1D658_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26952.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Chaperone protein DnaJ"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26952.1"}],"value":"dnaJ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26952.1"}],"value":"PQQ29_07565"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Binds 2 Zn(2+) ions per monomer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Belongs to the DnaJ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"J","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50076"}]},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"CR-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51188"}]},{"type":"Repeat","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"CXXCXGXG motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}]},{"type":"Repeat","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"CXXCXGXG motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}]},{"type":"Repeat","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"CXXCXGXG motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}]},{"type":"Repeat","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"CXXCXGXG motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}]},{"type":"Zinc finger","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"CR-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00546"}]},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022705"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"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_01152"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0346","category":"Biological process","name":"Stress response"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01152"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26952.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26952.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT26952.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_045554174.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"GeneID","id":"93234890","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:InterPro"}]},{"database":"GO","id":"GO:0031072","properties":[{"key":"GoTerm","value":"F:heat shock protein binding"},{"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:0042026","properties":[{"key":"GoTerm","value":"P:protein refolding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009408","properties":[{"key":"GoTerm","value":"P:response to heat"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06257","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd10747","properties":[{"key":"EntryName","value":"DnaJ_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd10719","properties":[{"key":"EntryName","value":"DnaJ_zf"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.110:FF:000031","properties":[{"key":"EntryName","value":"Molecular chaperone DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.260.20:FF:000004","properties":[{"key":"EntryName","value":"Molecular chaperone DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.260.20:FF:000009","properties":[{"key":"EntryName","value":"Putative Mitochondrial DnaJ chaperone"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.20.20.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.287.110","properties":[{"key":"EntryName","value":"DnaJ domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.260.20","properties":[{"key":"EntryName","value":"Urease metallochaperone UreE, N-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01152","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012724","properties":[{"key":"EntryName","value":"DnaJ"}]},{"database":"InterPro","id":"IPR002939","properties":[{"key":"EntryName","value":"DnaJ_C"}]},{"database":"InterPro","id":"IPR001623","properties":[{"key":"EntryName","value":"DnaJ_domain"}]},{"database":"InterPro","id":"IPR018253","properties":[{"key":"EntryName","value":"DnaJ_domain_CS"}]},{"database":"InterPro","id":"IPR008971","properties":[{"key":"EntryName","value":"HSP40/DnaJ_pept-bd"}]},{"database":"InterPro","id":"IPR001305","properties":[{"key":"EntryName","value":"HSP_DnaJ_Cys-rich_dom"}]},{"database":"InterPro","id":"IPR036410","properties":[{"key":"EntryName","value":"HSP_DnaJ_Cys-rich_dom_sf"}]},{"database":"InterPro","id":"IPR036869","properties":[{"key":"EntryName","value":"J_dom_sf"}]},{"database":"NCBIfam","id":"NF008035","properties":[{"key":"EntryName","value":"dnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010869","properties":[{"key":"EntryName","value":"dnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010873","properties":[{"key":"EntryName","value":"dnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02349","properties":[{"key":"EntryName","value":"DnaJ_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43096:SF48","properties":[{"key":"EntryName","value":"CHAPERONE PROTEIN DNAJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43096","properties":[{"key":"EntryName","value":"DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00226","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01556","properties":[{"key":"EntryName","value":"DnaJ_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF27439","properties":[{"key":"EntryName","value":"DnaJ_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00684","properties":[{"key":"EntryName","value":"DnaJ_CXXCXGXG"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00625","properties":[{"key":"EntryName","value":"JDOMAIN"}]},{"database":"SMART","id":"SM00271","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46565","properties":[{"key":"EntryName","value":"Chaperone J-domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57938","properties":[{"key":"EntryName","value":"DnaJ/Hsp40 cysteine-rich domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49493","properties":[{"key":"EntryName","value":"HSP40/DnaJ peptide-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00636","properties":[{"key":"EntryName","value":"DNAJ_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50076","properties":[{"key":"EntryName","value":"DNAJ_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51188","properties":[{"key":"EntryName","value":"ZF_CR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKRDYYEVLGVSKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGAGGGFGGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD","length":376,"molWeight":41006,"crc64":"92BC96EC53054A7D","md5":"E290851828F4786A2182372E648531C8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Repeat":4,"Zinc finger":1,"Binding site":8},"uniParcId":"UPI0005EDE65E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D671","uniProtkbId":"A0ACH1D671_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26967.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"Shikimate dehydrogenase (NADP(+))"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"SDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"1.1.1.25"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26967.1"}],"value":"aroE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26967.1"}],"value":"PQQ29_07645"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17737"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049442"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004871"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"value":"Belongs to the shikimate dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]},{"type":"Domain","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01488"}]},{"type":"Domain","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"SDH C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18317"}]},{"type":"Active site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:36208"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"shikimate","id":"ChEBI:CHEBI:36208"}},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:36208"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"shikimate","id":"ChEBI:CHEBI:36208"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:36208"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"shikimate","id":"ChEBI:CHEBI:36208"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:36208"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"shikimate","id":"ChEBI:CHEBI:36208"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:36208"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"shikimate","id":"ChEBI:CHEBI:36208"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:36208"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"ligand":{"name":"shikimate","id":"ChEBI:CHEBI:36208"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00222"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26967.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26967.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT26967.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010991578.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"GeneID","id":"51669327","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019632","properties":[{"key":"GoTerm","value":"P:shikimate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01065","properties":[{"key":"EntryName","value":"NAD_bind_Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, 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_00222","properties":[{"key":"EntryName","value":"Shikimate_DH_AroE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR041121","properties":[{"key":"EntryName","value":"SDH_C"}]},{"database":"InterPro","id":"IPR011342","properties":[{"key":"EntryName","value":"Shikimate_DH"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR022893","properties":[{"key":"EntryName","value":"Shikimate_DH_fam"}]},{"database":"InterPro","id":"IPR006151","properties":[{"key":"EntryName","value":"Shikm_DH/Glu-tRNA_Rdtase"}]},{"database":"NCBIfam","id":"NF001310","properties":[{"key":"EntryName","value":"aroE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00507","properties":[{"key":"EntryName","value":"aroE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21089:SF1","properties":[{"key":"EntryName","value":"BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21089","properties":[{"key":"EntryName","value":"SHIKIMATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18317","properties":[{"key":"EntryName","value":"SDH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01488","properties":[{"key":"EntryName","value":"Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08501","properties":[{"key":"EntryName","value":"Shikimate_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKYVVIGNPIRHSLSPAMQNRIFQELGMNAEYNSVLIEEDTFETEIKKLMDSGVRGFNITTPFKERILPFLDELEDLAAASGAVNTVLRKDGKWYGFNTDGKGYLEGLEEIRSITKDDSILITGAGGASKAIYLALKSHTEAKITVANRTTEKAIEMTKDNDNHHAMTLEQAEKELADFTIIIQTTSIGLEASKNKSPISLSNLTKGTICSDIIYNPAETAFLKEAKKNGAITQNGLPMFVNQGALAFEIWTGIKPERSMMKEAVLEQLGGN","length":273,"molWeight":30053,"crc64":"FD9EB653C26D6E26","md5":"60651A97FA610058FAB1673C1D4569BB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3,"Active site":1,"Binding site":11},"uniParcId":"UPI00000CC5AD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D689","uniProtkbId":"A0ACH1D689_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27000.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011893"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Adenine phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"APRT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011893"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"2.4.2.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"apt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27000.1"}],"value":"PQQ29_07820"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16609"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.4.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000868"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008391"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"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_00004"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27000.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27000.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27000.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003723528.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000001.1"}]},{"database":"SMR","id":"A0ACH1D689","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669361","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0002055","properties":[{"key":"GoTerm","value":"F:adenine binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003999","properties":[{"key":"GoTerm","value":"F:adenine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006168","properties":[{"key":"GoTerm","value":"P:adenine salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044209","properties":[{"key":"GoTerm","value":"P:AMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006166","properties":[{"key":"GoTerm","value":"P:purine ribonucleoside salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000004","properties":[{"key":"EntryName","value":"Adenine phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00004","properties":[{"key":"EntryName","value":"Aden_phosphoribosyltr"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005764","properties":[{"key":"EntryName","value":"Ade_phspho_trans"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR050054","properties":[{"key":"EntryName","value":"UPRTase/APRTase"}]},{"database":"NCBIfam","id":"TIGR01090","properties":[{"key":"EntryName","value":"apt"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002633","properties":[{"key":"EntryName","value":"PRK02304.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002634","properties":[{"key":"EntryName","value":"PRK02304.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002636","properties":[{"key":"EntryName","value":"PRK02304.1-5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315:SF3","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEIKDLQDYVAIVNDWPKKGIVFKDITPLMNDGEAYRFATDKIVEYAKELKIDIIVGPEARGFIIGCPVAYALGIGFAPVRKPGKLPRETIEMEYDLEYGTNKLSMHSDAIKPGQRVLITDDLLATGGTIEATIKLVEELGGIVAGCAFLIELKELEGHKKLNGYDRLILMKL","length":173,"molWeight":19182,"crc64":"9E5C25F0A6E99FDA","md5":"0E304B731876A7417408FF629C0535C4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0000055382"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6B0","uniProtkbId":"A0ACH1D6B0_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27032.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Porphobilinogen deaminase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"PBG"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"2.5.1.61"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Hydroxymethylbilane synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"HMBS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Pre-uroporphyrinogen synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27032.1"}],"value":"hemC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27032.1"}],"value":"PQQ29_07980"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002869"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13185"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57845"},{"database":"ChEBI","id":"CHEBI:58126"}],"ecNumber":"2.5.1.61","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048169"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"dipyrromethane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60342"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Binds 1 dipyrromethane group covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004735"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"The porphobilinogen subunits are added to the dipyrromethane group"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005638"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Belongs to the HMBS family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01379"}]},{"type":"Domain","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03900"}]},{"type":"Modified residue","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"S-(dipyrrolylmethanemethyl)cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27032.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27032.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27032.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_187984128.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"GeneID","id":"93234973","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0004418","properties":[{"key":"GoTerm","value":"F:hydroxymethylbilane synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd13646","properties":[{"key":"EntryName","value":"PBP2_EcHMBS_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.160.40:FF:000001","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.190.10:FF:000004","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.190.10:FF:000005","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.160.40","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00260","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000860","properties":[{"key":"EntryName","value":"HemC"}]},{"database":"InterPro","id":"IPR022419","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_cofac_BS"}]},{"database":"InterPro","id":"IPR022417","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_N"}]},{"database":"InterPro","id":"IPR022418","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C"}]},{"database":"InterPro","id":"IPR036803","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C_sf"}]},{"database":"NCBIfam","id":"TIGR00212","properties":[{"key":"EntryName","value":"hemC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557:SF0","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01379","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03900","properties":[{"key":"EntryName","value":"Porphobil_deamC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001438","properties":[{"key":"EntryName","value":"4pyrrol_synth_OHMeBilane_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00151","properties":[{"key":"EntryName","value":"PORPHBDMNASE"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54782","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00533","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN_DEAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRKIIVGSRRSKLALTQSNWVIKKLKENYPEIDFEIKEIVTKGDRILDVTLSKVGGKGLFVSEVEQALSDEVIDFAVHSMKDVPSSLKDGLVIGAIPKRESPLDCFVFNEVSTLDDLPKGAVIGTSSLRRAAQLLKHRPDFVVKPIRGNIDTRLQKLHAENFDAIILAKAGLARMGWLENTSLKLEDISPELCLPAVGQGALAIECRETDLQICDMLASIHHEETGICVEAERVFLKKLNGGCEIPIAGFATKTGDSVHFKGLVGNSDGSIILESERTGASPAEIGNQVAEELLSEGADTIIKELRNI","length":309,"molWeight":33678,"crc64":"143EC5F20C6C14A9","md5":"D327869198E0ABCB08850EC82914816A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Modified residue":1},"uniParcId":"UPI00165D6987"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6D3","uniProtkbId":"A0ACH1D6D3_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27027.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019357"}],"value":"Dihydrofolate synthase/folylpolyglutamate synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013023"}],"value":"6.3.2.12"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013025"}],"value":"6.3.2.17"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030592"}],"value":"Tetrahydrofolylpolyglutamate synthase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27027.1"}],"value":"PQQ29_07955"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10580"},{"database":"Rhea","id":"RHEA-COMP:14738"},{"database":"Rhea","id":"RHEA-COMP:14740"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:141005"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047493"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7,8-dihydropteroate + L-glutamate + ATP = 7,8-dihydrofolate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23584"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17839"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57451"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049161"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004799"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005150"}],"value":"Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008276"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001563"}],"value":"Belongs to the folylpolyglutamate synthase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001563"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022909"}],"id":"KW-0289","category":"Biological process","name":"Folate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001563"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001563"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27027.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27027.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27027.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_187984126.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"GeneID","id":"93234968","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:InterPro"}]},{"database":"GO","id":"GO:0008841","properties":[{"key":"GoTerm","value":"F:dihydrofolate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004326","properties":[{"key":"GoTerm","value":"F:tetrahydrofolylpolyglutamate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"3.40.1190.10:FF:000004","properties":[{"key":"EntryName","value":"Dihydrofolate synthase/folylpolyglutamate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001645","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth"}]},{"database":"InterPro","id":"IPR018109","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth_CS"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"NCBIfam","id":"TIGR01499","properties":[{"key":"EntryName","value":"folC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11136:SF0","properties":[{"key":"EntryName","value":"DIHYDROFOLATE SYNTHETASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11136","properties":[{"key":"EntryName","value":"FOLYLPOLYGLUTAMATE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001563","properties":[{"key":"EntryName","value":"Folylpolyglu_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01012","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALKSYQEALDWIHGTLRLGIKPGLARMEYIMEKLNHPEKANKWLHIAGTNGKGSTLTFIRSSLEEAGYKTGTFTSPYIETFNERISVNGIPVSDQMIVDLANRIKPIAEELEKTVYGPPSEFEIITAMMFLCFAEYEPIDIGIIEVGLGGRLDSTNVLTPLISVITTIGMDHMEFLGNSIEQIAGEKAGIIKPGIPVISGVIQKEAQEVIINNAVRNNSNVAWLNKDFFIQNRGDEITFRTSHGDEIPDITIGLLGIHQLNNAAVAIKVLQYLNTFSSYEINQSAIKQGLKKAFWPGRMELLDVKPFIMLDGAHNPEGVKTFADSIKTYPGHKKIIVSILKDKNYQEMIALLKTIPDTEILLTTFDYPRAMSDYEVTQIGTIEGISTNPNWKQALDDIKEIKNDTKFFVTGSLYFISEVRKYLLTSHN","length":429,"molWeight":47977,"crc64":"2EBF1653AD48B007","md5":"BD1581304FC96B496831FB2C3CC16DE6"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI0010B8201B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6G3","uniProtkbId":"A0ACH1D6G3_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27072.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Arginine biosynthesis bifunctional protein ArgJ"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Glutamate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"2.3.1.35"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Ornithine acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"OATase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Ornithine transacetylase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Amino-acid acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"2.3.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"N-acetylglutamate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"AGSase"}]}]}],"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Arginine biosynthesis bifunctional protein ArgJ alpha chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Arginine biosynthesis bifunctional protein ArgJ beta chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27072.1"}],"value":"argJ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27072.1"}],"value":"PQQ29_08185"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24292"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"}],"ecNumber":"2.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15349"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:46911"},{"database":"ChEBI","id":"CHEBI:57805"}],"ecNumber":"2.3.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Heterotetramer of two alpha and two beta chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006774"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Belongs to the ArgJ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Arginine biosynthesis bifunctional protein ArgJ alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"featureId":"PRO_5048382310"},{"type":"Chain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Arginine biosynthesis bifunctional protein ArgJ beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"featureId":"PRO_5048382311"},{"type":"Active site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":398,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]},{"type":"Site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]},{"type":"Site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Cleavage; by autolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"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_01106"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022813"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0068","category":"PTM","name":"Autocatalytic cleavage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"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_01106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27072.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27072.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27072.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010991622.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM135728.1"}]},{"database":"SMR","id":"A0ACH1D6G3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669434","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0004042","properties":[{"key":"GoTerm","value":"F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004358","properties":[{"key":"GoTerm","value":"F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor"},{"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:0006592","properties":[{"key":"GoTerm","value":"P:L-ornithine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02152","properties":[{"key":"EntryName","value":"OAT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.340:FF:000001","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.2330.10:FF:000001","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.70.12:FF:000002","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.2330.10","properties":[{"key":"EntryName","value":"arginine biosynthesis bifunctional protein suprefamily"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.340","properties":[{"key":"EntryName","value":"ArgJ beta chain, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.70.12","properties":[{"key":"EntryName","value":"L-amino peptidase D-ALA esterase/amidase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01106","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002813","properties":[{"key":"EntryName","value":"Arg_biosynth_ArgJ"}]},{"database":"InterPro","id":"IPR016117","properties":[{"key":"EntryName","value":"ArgJ-like_dom_sf"}]},{"database":"InterPro","id":"IPR042195","properties":[{"key":"EntryName","value":"ArgJ_beta_C"}]},{"database":"NCBIfam","id":"NF003802","properties":[{"key":"EntryName","value":"argJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00120","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23100","properties":[{"key":"EntryName","value":"ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23100:SF0","properties":[{"key":"EntryName","value":"ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01960","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56266","properties":[{"key":"EntryName","value":"DmpA/ArgJ-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MELIKGNIASPKGFYADGKHAGLKRKRNDIGWIYSEVPANSAAVYTMNQMQAAPIFVTKDSFKNSAKLQAIIVNSGNANAVTGNQGMLDALSMRAKTAEKLAIPMDTVAVASTGIIGEMLPMDKIMTGIDLLEKQTGNAADFEEAILTTDTFQKQISFQTEIGGKTVTMSGVAKGSGMIHPNMATMLAFITTDAAIPAELLQKLLKIKVDKTFNQITVDGDTSTNDMVVVMANGCAENPLIQEGTADFEKFAAMFQAVTEHLAKSIARDGEGATKLIEVQVKGATKTEDARMIAKKIVSSSLVKTAAFGGDGNWGRIICAIGYSGGRFAPDNITIKIGGIEILNHSSQTIFNQQALDAYLEEEHIVIEVDLHIGLESGTAWGCDLSYEYVKINACYRT","length":398,"molWeight":42693,"crc64":"86760EF9FF50A46C","md5":"278E6154A67282718BE5DE8C7ECAF580"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":2,"Active site":1,"Binding site":6,"Site":3},"uniParcId":"UPI00000CC5F7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6H8","uniProtkbId":"A0ACH1D6H8_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017068"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Enolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012058"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"4.2.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"2-phospho-D-glycerate hydro-lyase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"2-phosphoglycerate dehydratase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"}],"value":"eno"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"}],"value":"PQQ29_00110"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10164"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58289"},{"database":"ChEBI","id":"CHEBI:58702"}],"ecNumber":"4.2.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048951"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:10165"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048951"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Binds a second Mg(2+) ion via substrate during catalysis."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005031"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Fractions of enolase are present in both the cytoplasm and on the cell surface"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Cell surface","id":"SL-0310"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009604"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Belongs to the enolase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Enolase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01193"}]},{"type":"Domain","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Enolase C-terminal TIM barrel","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01192"}]},{"type":"Active site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}]},{"type":"Active site","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}]},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"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_00318"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"value":"pATCC33090_1","geneEncodingType":"Plasmid"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"}],"id":"KW-0614","category":"Technical term","name":"Plasmid"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"}],"value":"ATCC 33090","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"}],"value":"pATCC33090_1","type":"PLASMID"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26936.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117228","properties":[{"key":"ProteinId","value":"WCT26936.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_064659124.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP102628.1"}]},{"database":"GeneID","id":"93233400","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","properties":[{"key":"Component","value":"Plasmid pATCC33090_1"}]},{"database":"GO","id":"GO:0009986","properties":[{"key":"GoTerm","value":"C:cell surface"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000015","properties":[{"key":"GoTerm","value":"C:phosphopyruvate hydratase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004634","properties":[{"key":"GoTerm","value":"F:phosphopyruvate hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03313","properties":[{"key":"EntryName","value":"enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.120","properties":[{"key":"EntryName","value":"Enolase-like C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.390.10","properties":[{"key":"EntryName","value":"Enolase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00318","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000941","properties":[{"key":"EntryName","value":"Enolase"}]},{"database":"InterPro","id":"IPR036849","properties":[{"key":"EntryName","value":"Enolase-like_C_sf"}]},{"database":"InterPro","id":"IPR029017","properties":[{"key":"EntryName","value":"Enolase-like_N"}]},{"database":"InterPro","id":"IPR020810","properties":[{"key":"EntryName","value":"Enolase_C"}]},{"database":"InterPro","id":"IPR020809","properties":[{"key":"EntryName","value":"Enolase_CS"}]},{"database":"InterPro","id":"IPR020811","properties":[{"key":"EntryName","value":"Enolase_N"}]},{"database":"NCBIfam","id":"TIGR01060","properties":[{"key":"EntryName","value":"eno"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11902","properties":[{"key":"EntryName","value":"ENOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11902:SF1","properties":[{"key":"EntryName","value":"ENOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00113","properties":[{"key":"EntryName","value":"Enolase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03952","properties":[{"key":"EntryName","value":"Enolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001400","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00148","properties":[{"key":"EntryName","value":"ENOLASE"}]},{"database":"SFLD","id":"SFLDF00002","properties":[{"key":"EntryName","value":"enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG00178","properties":[{"key":"EntryName","value":"enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00001","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01192","properties":[{"key":"EntryName","value":"Enolase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01193","properties":[{"key":"EntryName","value":"Enolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51604","properties":[{"key":"EntryName","value":"Enolase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54826","properties":[{"key":"EntryName","value":"Enolase N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00164","properties":[{"key":"EntryName","value":"ENOLASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKTVYFISIYPTVEVDVHLTDGTIGRAAVPSGASTGDREAVELRDGGDRLQGLGVKTAVQNVNLTLNDALVGISPFNQREIDHKMIELDGTANKSRLGANAILGVSMAVARAAAKSEAVPLYRYLGGIDLELPRPFFNVINGGKHADSGIDVQEFLITPIAALSFREGLESIADVYHTLKKLLSKRGLATSVGDEGGFAPRLASTEEALEVLVEAIKKAGYKPGEDIAIAMDPAASEFSENNTYYFEGKQLSSEEMIHYYEHLVQEFPIISIEDGLSEHDWEGFKLMTEKLGNKVQLVGDDIFVTNPIIFQQGIDKGIGNAILIKLNQIGTVTETIDKINLARKNNYATMISHRSGETGDTFIADFAVAMHAGQIKTGSIARSERVEKYNQFLRIEEELAKIK","length":404,"molWeight":44105,"crc64":"79ED6459F7243DF7","md5":"F09B6F6BA463711619844FEA7E1273A4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":8},"uniParcId":"UPI0007E3596C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6I0","uniProtkbId":"A0ACH1D6I0_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27102.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27102.1"}],"value":"PQQ29_08340"}]}],"comments":[{"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"},{"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":"HAMAP-Rule","id":"MF_01965"}]}},{"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":"HAMAP-Rule","id":"MF_01965"}]}},{"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"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"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":101,"modifier":"EXACT"},"end":{"value":101,"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":152,"modifier":"EXACT"},"end":{"value":152,"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":183,"modifier":"EXACT"},"end":{"value":187,"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":211,"modifier":"EXACT"},"end":{"value":211,"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":212,"modifier":"EXACT"},"end":{"value":212,"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":"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":"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:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27102.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27102.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27102.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003772085.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000001.1"}]},{"database":"GeneID","id":"51669465","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"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":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKITPKAMCAWIPKREDETHKGDYGRVLIVAGNKQFGGAAIMAAEACVKSGAGLTTVASDSVNRPALQTRIPECMFIDYENITSLSEQINHFDTILIGPGLGLDAYAEEIFRLVLQNSTEHQQLIIDGDGITIYAKGENPHPAAKLTFTPHAGEWERLKALAPEAETPTDVALHIDATIVLKGHRTKVYSGESAWQNMYGTPAMATGGMGDTLAGTICGLMAQTEKPLTGTLAAVFLHSYIGEILAKKRYVVLPTEIAEELPTYLKIFSETDEHA","length":276,"molWeight":29914,"crc64":"BEAC9F8D11B85476","md5":"06912A9D481C882E245AF65BF4D280F2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":6},"uniParcId":"UPI00000CC611"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6I3","uniProtkbId":"A0ACH1D6I3_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27152.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"SEPHCHC synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"2.2.1.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Menaquinone biosynthesis protein MenD"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27152.1"}],"value":"menD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27152.1"}],"value":"PQQ29_08595"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"isochorismate + 2-oxoglutarate + H(+) = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25593"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29780"},{"database":"ChEBI","id":"CHEBI:58818"}],"ecNumber":"2.2.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Quinol/quinone metabolism; menaquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"value":"Belongs to the TPP enzyme family. MenD subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Menaquinone biosynthesis protein MenD middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16582"}]},{"type":"Domain","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":554,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"id":"KW-0474","category":"Biological process","name":"Menaquinone biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"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_01659"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01659"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27152.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27152.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27152.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003772171.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000001.1"}]},{"database":"SMR","id":"A0ACH1D6I3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669588","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0070204","properties":[{"key":"GoTerm","value":"F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009234","properties":[{"key":"GoTerm","value":"P:menaquinone biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07037","properties":[{"key":"EntryName","value":"TPP_PYR_MenD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02009","properties":[{"key":"EntryName","value":"TPP_SHCHC_synthase"},{"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_01659","properties":[{"key":"EntryName","value":"MenD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR004433","properties":[{"key":"EntryName","value":"MenaQ_synth_MenD"}]},{"database":"InterPro","id":"IPR032264","properties":[{"key":"EntryName","value":"MenD_middle"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"NCBIfam","id":"TIGR00173","properties":[{"key":"EntryName","value":"menD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42916","properties":[{"key":"EntryName","value":"2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42916:SF1","properties":[{"key":"EntryName","value":"PROTEIN PHYLLO, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16582","properties":[{"key":"EntryName","value":"TPP_enzyme_M_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF004983","properties":[{"key":"EntryName","value":"MenD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTNHEQVLTDYLAAFIEELVQAGVKEAIISPGSRSTPLALMMAEHPTLKIYVDVDERSAGFFALGLAKASKRPVVLLCTSGTAAANYFPAVVEANLSQIPLIVLTADRPHELRNVGAPQAMDQLHLYGSHVKDFTDMALPENSDEMLRYAKWHSSRAVDIAMKTPRGPVHLNFPLREPLVPILEPSPFTATGKKHHHVHIYYTHEVLDDSSIQKMVTECTGKKGVFVVGPIDKKELEQPMVDLAKKLGWPILADPLSGLRSYGAMDEVVIDQYDAFLKEADILDKLTPEVVIRFGSMPVSKPLKNWLEHLFGIRFYVVDPGAAWKDPIKAVTDMIHCDERFLLDIMQQNMPDDTKDASWLNRWTSYNQKAREIVLEEMANTTTLEEGKIVSELRRLLPDKAGLFIGNSMPIRDVDTYFSQIDKKIKMLANRGANGIDGVVSSALGASVVFQPMFLLIGDLSFYHDMNGLLMAKKYKMNLTIIIVNNDGGGIFSFLPQANEPKYFESLFGTSTELDFRFAAAFYDADYHEAKSVDSLEEAIDKASYHKGLDIIEVKTNRHENKANHQALWEKIATALKALD","length":580,"molWeight":64852,"crc64":"D41C056CC9FB4E0F","md5":"E17951DC0473B3FDF1E94F7FEE60839C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI00000CC66C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6I6","uniProtkbId":"A0ACH1D6I6_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27150.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"1,4-dihydroxy-2-naphthoyl-CoA synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"DHNA-CoA synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"4.1.3.36"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27150.1"}],"value":"menB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27150.1"}],"value":"PQQ29_08585"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26562"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57364"},{"database":"ChEBI","id":"CHEBI:58897"}],"ecNumber":"4.1.3.36","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000177"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"hydrogencarbonate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00053033"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:17544"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"Quinol/quinone metabolism; menaquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00378"}]},{"type":"Region","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17544"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"hydrogencarbonate","id":"ChEBI:CHEBI:17544"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"ligand":{"name":"substrate","note":"ligand shared between two neighboring subunits"}},{"type":"Site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}]},{"type":"Site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01934"}],"id":"KW-0474","category":"Biological process","name":"Menaquinone biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27150.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27150.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27150.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003723264.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAFVD010000010.1"}]},{"database":"GeneID","id":"51669586","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0008935","properties":[{"key":"GoTerm","value":"F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009234","properties":[{"key":"GoTerm","value":"P:menaquinone biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.12.10:FF:000003","properties":[{"key":"EntryName","value":"1,4-dihydroxy-2-naphthoyl-CoA synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000003","properties":[{"key":"EntryName","value":"1,4-dihydroxy-2-naphthoyl-CoA synthase"},{"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":"1.10.12.10","properties":[{"key":"EntryName","value":"Lyase 2-enoyl-coa Hydratase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01934","properties":[{"key":"EntryName","value":"MenB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR010198","properties":[{"key":"EntryName","value":"DHNA-CoA_synthase_MenB"}]},{"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":"IPR014748","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra_C"}]},{"database":"NCBIfam","id":"NF005637","properties":[{"key":"EntryName","value":"menB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01929","properties":[{"key":"EntryName","value":"menB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43113:SF1","properties":[{"key":"EntryName","value":"1,4-DIHYDROXY-2-NAPHTHOYL-COA SYNTHASE, PEROXISOMAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43113","properties":[{"key":"EntryName","value":"NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00166","properties":[{"key":"EntryName","value":"ENOYL_COA_HYDRATASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFNWQTEKVYEEIKYESYEGIAKITINRPEVHNAFTPKTVTEMIDAFNLARDNSDLGVIILTGEGEKAFCSGGDQKVRGHGGYVGDDQIPRLNVLDLQRLIRVIPKPVIAMVAGWSIGGGNVLQLVCDLTIAADNAKFGQTGPNVGSFDAGYGSGYLARVIGHKKAKEVWFMCRQYTADEALEMGWINTVVPVADLEKETVAWAKEMLQKSPTALRFIKAAFNADTDGLAGIQQLAGDATLLYYTTDEAKEGRDAFKEKRDPDFDQFPKFP","length":272,"molWeight":30025,"crc64":"3099D906529E52A8","md5":"B901E642028B438A21CB8694F7F36C13"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":8,"Site":2},"uniParcId":"UPI00000CC66A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6L3","uniProtkbId":"A0ACH1D6L3_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26998.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"D-aminoacyl-tRNA deacylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"DTD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"3.1.1.96"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Gly-tRNA(Ala) deacylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"3.1.1.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26998.1"}],"value":"dtd"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26998.1"}],"value":"PQQ29_07810"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13953"},{"database":"Rhea","id":"RHEA-COMP:10123"},{"database":"Rhea","id":"RHEA-COMP:10124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:59871"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:79333"}],"ecNumber":"3.1.1.96","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53744"},{"database":"Rhea","id":"RHEA-COMP:9657"},{"database":"Rhea","id":"RHEA-COMP:13640"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78522"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009673"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Belongs to the DTD family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Motif","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Gly-cisPro motif, important for rejection of L-amino acids","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26998.1"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26998.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT26998.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT26998.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003762386.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAFVD010000014.1"}]},{"database":"SMR","id":"A0ACH1D6L3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"51669359","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0051500","properties":[{"key":"GoTerm","value":"F:D-tyrosyl-tRNA(Tyr) deacylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0106026","properties":[{"key":"GoTerm","value":"F:Gly-tRNA(Ala) deacylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043908","properties":[{"key":"GoTerm","value":"F:Ser(Gly)-tRNA(Ala) hydrolase 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:0019478","properties":[{"key":"GoTerm","value":"P:D-amino acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00563","properties":[{"key":"EntryName","value":"Dtyr_deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.80.10:FF:000001","properties":[{"key":"EntryName","value":"D-aminoacyl-tRNA deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.80.10","properties":[{"key":"EntryName","value":"D-tyrosyl-tRNA(Tyr) deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00518","properties":[{"key":"EntryName","value":"Deacylase_Dtd"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003732","properties":[{"key":"EntryName","value":"Daa-tRNA_deacyls_DTD"}]},{"database":"InterPro","id":"IPR023509","properties":[{"key":"EntryName","value":"DTD-like_sf"}]},{"database":"NCBIfam","id":"TIGR00256","properties":[{"key":"EntryName","value":"D-aminoacyl-tRNA deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10472:SF5","properties":[{"key":"EntryName","value":"D-AMINOACYL-TRNA DEACYLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10472","properties":[{"key":"EntryName","value":"D-TYROSYL-TRNA TYR DEACYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02580","properties":[{"key":"EntryName","value":"Tyr_Deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69500","properties":[{"key":"EntryName","value":"DTD-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVLLQRCYEASVRVEGEIISEIAGGLCLLVGFTHSDTEETVEYMAKKIIGLRVFEDESEKMNISLAERGGAILSVSQFTLYADVSRGKRPSFTKSAPGEKAEGLYNLFNNKLSDAGFIVETGVFGAFMDVKIVNNGPVTIMLDSEEMRK","length":150,"molWeight":16524,"crc64":"609BA27ED9C04B43","md5":"4CC384DE703F74746FC2311D65D560A8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Motif":1},"uniParcId":"UPI0000129935"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACH1D6M0","uniProtkbId":"A0ACH1D6M0_LISIO","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-06-10","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Listeria innocua","taxonId":1642,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27013.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Listeriaceae","Listeria"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"GTPase Obg"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"3.6.5.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"GTP-binding protein Obg"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27013.1"}],"value":"obgE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"obg"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27013.1"}],"value":"PQQ29_07885"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007699"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"value":"Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Obg","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51883"}]},{"type":"Domain","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"OBG-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51710"}]},{"type":"Domain","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"OCT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51881"}]},{"type":"Region","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001214687"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3IDLO1VM0F8KO","citationType":"submission","authors":["Johnson J.D.","Blankenship H.","Soehnlen M."],"title":"Long read genome assemblers struggle with small plasmids.","publicationDate":"JAN-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27013.1"}],"value":"ATCC 33090","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WCT27013.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP117229","properties":[{"key":"ProteinId","value":"WCT27013.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003767023.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AADHQU020000001.1"}]},{"database":"GeneID","id":"93234954","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001214687","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:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042254","properties":[{"key":"GoTerm","value":"P:ribosome biogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01898","properties":[{"key":"EntryName","value":"Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.70.210.12:FF:000001","properties":[{"key":"EntryName","value":"GTPase Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000515","properties":[{"key":"EntryName","value":"GTPase Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.350","properties":[{"key":"EntryName","value":"GTP-binding protein OBG, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.210.12","properties":[{"key":"EntryName","value":"GTP1/OBG domain"},{"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_01454","properties":[{"key":"EntryName","value":"GTPase_Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR031167","properties":[{"key":"EntryName","value":"G_OBG"}]},{"database":"InterPro","id":"IPR006073","properties":[{"key":"EntryName","value":"GTP-bd"}]},{"database":"InterPro","id":"IPR014100","properties":[{"key":"EntryName","value":"GTP-bd_Obg/CgtA"}]},{"database":"InterPro","id":"IPR036346","properties":[{"key":"EntryName","value":"GTP-bd_prot_GTP1/OBG_C_sf"}]},{"database":"InterPro","id":"IPR006074","properties":[{"key":"EntryName","value":"GTP1-OBG_CS"}]},{"database":"InterPro","id":"IPR006169","properties":[{"key":"EntryName","value":"GTP1_OBG_dom"}]},{"database":"InterPro","id":"IPR036726","properties":[{"key":"EntryName","value":"GTP1_OBG_dom_sf"}]},{"database":"InterPro","id":"IPR045086","properties":[{"key":"EntryName","value":"OBG_GTPase"}]},{"database":"InterPro","id":"IPR015349","properties":[{"key":"EntryName","value":"OCT_dom"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005225","properties":[{"key":"EntryName","value":"Small_GTP-bd"}]},{"database":"NCBIfam","id":"TIGR02729","properties":[{"key":"EntryName","value":"Obg_CgtA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR03595","properties":[{"key":"EntryName","value":"Obg_CgtA_exten"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008954","properties":[{"key":"EntryName","value":"obgE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008955","properties":[{"key":"EntryName","value":"obgE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008956","properties":[{"key":"EntryName","value":"obgE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00231","properties":[{"key":"EntryName","value":"small_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11702","properties":[{"key":"EntryName","value":"DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11702:SF31","properties":[{"key":"EntryName","value":"MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09269","properties":[{"key":"EntryName","value":"DUF1967"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01018","properties":[{"key":"EntryName","value":"GTP1_OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01926","properties":[{"key":"EntryName","value":"MMR_HSR1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002401","properties":[{"key":"EntryName","value":"GTP_bd_Obg/CgtA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00326","properties":[{"key":"EntryName","value":"GTP1OBG"}]},{"database":"SUPFAM","id":"SSF102741","properties":[{"key":"EntryName","value":"Obg GTP-binding protein C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF82051","properties":[{"key":"EntryName","value":"Obg GTP-binding protein N-terminal domain"},{"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":"PS51710","properties":[{"key":"EntryName","value":"G_OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00905","properties":[{"key":"EntryName","value":"GTP1_OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51883","properties":[{"key":"EntryName","value":"OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51881","properties":[{"key":"EntryName","value":"OCT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFVDQVKIYVKAGNGGDGMVAFRREKFVPNGGPAGGDGGKGADVVFVVDEGLRTLVDFRFKRIFKAEHGEHGMSKSMHGRGAEDLVVKVPQGTIVKDIDTGEIIADLVAHGQRAVIAKAGRGGRGNKRFATPANPAPELSENGEPGQERNVQLELKVLADVGLVGFPSVGKSTLLSVVSAARPKIAAYHFTTIVPNLGMVDAGDGRSFVMADLPGLIEGASQGVGLGHQFLRHIERTRVIVHVIDMSGSEGRVPYEDYMAINNELEQYNLRLMERPQIIVANKMDMPDAEENLKEFKTKIAEDIPVFPISAVTKTGLRELLLAIADKLETTPEFPLNEILEQEDEDTVLYKYVAEEPDFEITREPDGTFVLSGAKIERLFTMTNFERDASISRFARQLRAMGVDEALRKRGAKDGDIVRLLDYEFEFMD","length":429,"molWeight":47147,"crc64":"5F8C6BD93E83DB17","md5":"915069D8371C94D865A5EB28B8B3A7C5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":1,"Binding site":7},"uniParcId":"UPI0001EBB704"}}]}