{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P37766","secondaryAccessions":["P76199","P76898"],"uniProtkbId":"YDIF_ECOLI","entryAudit":{"firstPublicDate":"1994-10-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2000-12-01","entryVersion":143,"sequenceVersion":3},"annotationScore":3.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"36333310"}],"value":"Acetate CoA-transferase YdiF"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}],"value":"2.8.3.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"36333310"}],"value":"Lactyl-coenzyme A-transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}],"value":"2.8.3.-"}]},{"fullName":{"value":"Short-chain acyl-CoA:acetate CoA-transferase"}}]},"genes":[{"geneName":{"value":"ydiF"},"orderedLocusNames":[{"value":"b1694"},{"value":"JW1684"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}],"value":"CoA transferase that catalyzes the formation of acetyl-CoA from acetate and the formation of lactyl-CoA from lactate (PubMed:36333310). Lactyl-CoA can be used for lysine lactylation (Kla), which influences metabolism and biosynthesis (PubMed:36333310)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an acyl-CoA + acetate = a carboxylate + acetyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13381"},{"database":"ChEBI","id":"CHEBI:29067"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:58342"}],"ecNumber":"2.8.3.8","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetoacetate + acetyl-CoA = acetoacetyl-CoA + acetate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27806"},{"database":"ChEBI","id":"CHEBI:13705"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:57286"},{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetoacetyl-CoA + (S)-lactate = (S)-lactoyl-CoA + acetoacetate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:86711"},{"database":"ChEBI","id":"CHEBI:13705"},{"database":"ChEBI","id":"CHEBI:16651"},{"database":"ChEBI","id":"CHEBI:57286"},{"database":"ChEBI","id":"CHEBI:231528"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:86712"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36333310"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8X5X6"}],"value":"Homotetramer; dimer of dimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8X5X6"}],"value":"Formation of the covalent enzyme-CoA thioester intermediate proceeds via an unstable anhydride species formed between the carboxylate group of the catalytic glutamate of the enzyme and the carbonyl carbon of the thioester linkage of the substrate"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the 3-oxoacid CoA-transferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":531,"modifier":"EXACT"}},"description":"Acetate CoA-transferase YdiF","featureId":"PRO_0000168990"},{"type":"Active site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"5-glutamyl coenzyme A thioester intermediate","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8X5X6"}]}],"keywords":[{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9097039","citationType":"journal article","authors":["Aiba H.","Baba T.","Fujita K.","Hayashi K.","Inada T.","Isono K.","Itoh T.","Kasai H.","Kashimoto K.","Kimura S.","Kitakawa M.","Kitagawa M.","Makino K.","Miki T.","Mizobuchi K.","Mori H.","Mori T.","Motomura K.","Nakade S.","Nakamura Y.","Nashimoto H.","Nishio Y.","Oshima T.","Saito N.","Sampei G.","Seki Y.","Sivasundaram S.","Tagami H.","Takeda J.","Takemoto K.","Takeuchi Y.","Wada C.","Yamamoto Y.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"9097039"},{"database":"DOI","id":"10.1093/dnares/3.6.363"}],"title":"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.","publicationDate":"1996","journal":"DNA Res.","firstPage":"363","lastPage":"377","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"3541912","citationType":"journal article","authors":["Duncan K.","Chaudhuri S.","Campbell M.S.","Coggins J.R."],"citationCrossReferences":[{"database":"PubMed","id":"3541912"},{"database":"DOI","id":"10.1042/bj2380475"}],"title":"The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase.","publicationDate":"1986","journal":"Biochem. J.","firstPage":"475","lastPage":"483","volume":"238"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64"]},{"referenceNumber":5,"citation":{"id":"7984428","citationType":"journal article","authors":["Borodovsky M.","Rudd K.E.","Koonin E.V."],"citationCrossReferences":[{"database":"PubMed","id":"7984428"},{"database":"DOI","id":"10.1093/nar/22.22.4756"}],"title":"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome.","publicationDate":"1994","journal":"Nucleic Acids Res.","firstPage":"4756","lastPage":"4767","volume":"22"},"referencePositions":["IDENTIFICATION"]},{"referenceNumber":6,"citation":{"id":"36333310","citationType":"journal article","authors":["Dong H.","Zhang J.","Zhang H.","Han Y.","Lu C.","Chen C.","Tan X.","Wang S.","Bai X.","Zhai G.","Tian S.","Zhang T.","Cheng Z.","Li E.","Xu L.","Zhang K."],"citationCrossReferences":[{"database":"PubMed","id":"36333310"},{"database":"DOI","id":"10.1038/s41467-022-34399-y"}],"title":"YiaC and CobB regulate lysine lactylation in Escherichia coli.","publicationDate":"2022","journal":"Nat. Commun.","firstPage":"6628","lastPage":"6628","volume":"13"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC74764.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA15447.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X04306","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"F64927","properties":[{"key":"EntryName","value":"F64927"}]},{"database":"RefSeq","id":"NP_416209.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000805700.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"AlphaFoldDB","id":"P37766","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P37766","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4260290","properties":[{"key":"Interactions","value":"23"}]},{"database":"BioGRID","id":"850571","properties":[{"key":"Interactions","value":"1"}]},{"database":"FunCoup","id":"P37766","properties":[{"key":"Number of interactors","value":"123"}]},{"database":"IntAct","id":"P37766","properties":[{"key":"Interactions","value":"2"}]},{"database":"STRING","id":"511145.b1694","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b1694","properties":[{"key":"Description","value":"-"}]},{"database":"DNASU","id":"946211","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC74764","properties":[{"key":"ProteinId","value":"AAC74764"},{"key":"GeneId","value":"b1694"}]},{"database":"GeneID","id":"946211","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW1684","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b1694","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.564","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB2328","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG4670","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_026774_4_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P37766","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"VKTMGQI","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"PhylomeDB","id":"P37766","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:EG12432-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P37766","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0008775","properties":[{"key":"GoTerm","value":"F:acetate CoA-transferase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0046952","properties":[{"key":"GoTerm","value":"P:ketone body catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051289","properties":[{"key":"GoTerm","value":"P:protein homotetramerization"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0046459","properties":[{"key":"GoTerm","value":"P:short-chain fatty acid metabolic process"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"FunFam","id":"3.40.1080.10:FF:000007","properties":[{"key":"EntryName","value":"Acetate CoA-transferase YdiF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1080.10:FF:000008","properties":[{"key":"EntryName","value":"Acetate CoA-transferase YdiF"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1080.10","properties":[{"key":"EntryName","value":"Glutaconate Coenzyme A-transferase"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR014388","properties":[{"key":"EntryName","value":"3-oxoacid_CoA-transferase"}]},{"database":"InterPro","id":"IPR004165","properties":[{"key":"EntryName","value":"CoA_trans_fam_I"}]},{"database":"InterPro","id":"IPR037171","properties":[{"key":"EntryName","value":"NagB/RpiA_transferase-like"}]},{"database":"PANTHER","id":"PTHR43293","properties":[{"key":"EntryName","value":"ACETATE COA-TRANSFERASE YDIF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43293:SF1","properties":[{"key":"EntryName","value":"ACETATE COA-TRANSFERASE YDIF"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01144","properties":[{"key":"EntryName","value":"CoA_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000858","properties":[{"key":"EntryName","value":"SCOT-t"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00882","properties":[{"key":"EntryName","value":"CoA_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100950","properties":[{"key":"EntryName","value":"NagB/RpiA/CoA transferase-like"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MKPVKPPRINGRVPVLSAQEAVNYIPDEATLCVLGAGGGILEATTLITALADKYKQTQTPRNLSIISPTGLGDRADRGISPLAQEGLVKWALCGHWGQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTKEDLIKLVEFDNKEYLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVVDPDQTQLYGGAPVNRFISGDFTLDDSTKLSLPLNQRKLVARRALFEMRKGAVGNVGVGIADGIGLVAREEGCADDFILTVETGPIGGITSQGIAFGANVNTRAILDMTSQFDFYHGGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSKKIIFCGTLTAGSLKTEITDGKLNIVQEGRVKKFIRELPEITFSGKIALERGLDVRYITERAVFTLKEDGLHLIEIAPGVDLQKDILDKMDFTPVISPELKLMDERLFIDAAMGFVLPEAAH","length":531,"molWeight":57562,"crc64":"E07A0D445015030D","md5":"555FCC3BB0C13A8B15DFF7EFDB719A87"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1},"uniParcId":"UPI000013A9D1"}}