{"metadata":{"accession":"PF05853","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR008567","hierarchy":null,"name":{"name":"beta-keto acid cleavage enzyme","short":"BKACE"},"description":[{"text":"<p>BKACE, beta-keto acid cleavage enzyme plays, a role in lysine degradation. In certain instances it catalyses the conversion of 3-keto-5-aminohexanoate and acetyl-CoA into acetoacetate and 3-aminobutyryl-CoA [[cite:PUB00056558]]. The family is found to have at least 14 slightly different potential new enzymatic activities, all of which can therefore be designated as beta-keto acid cleavage enzymes [[cite:PUB00103502]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00103502":{"PMID":24240508,"ISBN":null,"volume":"10","issue":"1","year":2014,"title":"Revealing the hidden functional diversity of an enzyme family.","URL":null,"raw_pages":"42-9","medline_journal":"Nat Chem Biol","ISO_journal":"Nat Chem Biol","authors":["Bastard K","Smith AA","Vergne-Vaxelaire C","Perret A","Zaparucha A","De Melo-Minardi R","Mariage A","Boutard M","Debard A","Lechaplais C","Pelle C","Pellouin V","Perchat N","Petit JL","Kreimeyer A","Medigue C","Weissenbach J","Artiguenave F","De Berardinis V","Vallenet D","Salanoubat M."],"DOI_URL":null},"PUB00056558":{"PMID":21632536,"ISBN":null,"volume":"286","issue":"31","year":2011,"title":"3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon Claisen-type condensation.","URL":null,"raw_pages":"27399-405","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Bellinzoni M","Bastard K","Perret A","Zaparucha A","Perchat N","Vergne C","Wagner T","de Melo-Minardi RC","Artiguenave F","Cohen GN","Weissenbach J","Salanoubat M","Alzari PM."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M111.253260"}},"set_info":{"accession":"CL0036","name":"TIM_barrel"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":34,"interactions":0,"matches":11865,"pathways":0,"proteins":11546,"proteomes":6039,"sets":1,"structural_models":{"alphafold":7293},"structures":25,"taxa":8565},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":158,"alignment:full":5866},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3no5","name":"Crystal structure of a Pfam DUF849 domain containing protein (Reut_A1631) from Ralstonia eutropha JMP134 at 1.90 A resolution"}}}