{"metadata":{"accession":"PF05708","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR024453","hierarchy":null,"name":{"name":"Permuted papain-like amidase enzyme, YaeF/YiiX, C92 family","short":"Peptidase_C92"},"description":[{"text":"<p>Amidase_YiiX is a family of permuted papain-like amidases. It has amidase specificity for the amide bond between a lipid and an amino acid (or peptide). From the structure, a tetramer, each monomer is made up of a layered alpha-beta fold with a central, 6-stranded, antiparallel beta-sheet that is protected by helices on either side. The catalytic Cys154 in UniProtKB:Q74NK7, PDB:3kw0, is located on the N-terminus of helix alphaF. The two additional helices located above Cys154 contribute to the formation of the active site, where the lysine ligand is bound [[cite:PUB00075488]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00075488":{"PMID":21799766,"ISBN":null,"volume":"6","issue":"7","year":2011,"title":"Structural analysis of papain-like NlpC/P60 superfamily enzymes with a circularly permuted topology reveals potential lipid binding sites.","URL":null,"raw_pages":"e22013","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Xu Q","Rawlings ND","Chiu HJ","Jaroszewski L","Klock HE","Knuth MW","Miller MD","Elsliger MA","Deacon AM","Godzik A","Lesley SA","Wilson IA."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0022013"}},"set_info":{"accession":"CL0125","name":"Peptidase_CA"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":32,"interactions":0,"matches":3260,"pathways":0,"proteins":3259,"proteomes":2690,"sets":1,"structural_models":{"alphafold":2152},"structures":2,"taxa":4781},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":13,"alignment:full":1580},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2if6","name":"Crystal structure of metalloprotein yiiX from Escherichia coli O157:H7, DUF1105"}}}