{"metadata":{"accession":"PF07313","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010846","hierarchy":null,"name":{"name":"N-acetylmuramoyl-L-alanine amidase-like","short":"AmiA-like"},"description":[{"text":"<p>This family includes N-acetylmuramoyl-L-alanine amidase (AMA) from Bacteroides uniformis and similar bacterial proteins. AmiA hydrolyses GlcNAc-1,6-anhydro-MurNAc-peptide into disaccharide and stem peptide. It shows an alpha/beta/alpha three-layered sandwich fold with a catalytic core that consists of a central five-stranded beta-sheet and four alpha-helices. It is structurally related to NlpC/P60 gamma- D-Glu-meso-diaminopimelic acid amidases [[cite:PUB00100890]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100890":{"PMID":25465128,"ISBN":null,"volume":"22","issue":"12","year":2014,"title":"Structure-guided functional characterization of DUF1460 reveals a highly specific NlpC/P60 amidase family.","URL":null,"raw_pages":"1799-1809","medline_journal":"Structure","ISO_journal":"Structure","authors":["Xu Q","Mengin-Lecreulx D","Patin D","Grant JC","Chiu HJ","Jaroszewski L","Knuth MW","Godzik A","Lesley SA","Elsliger MA","Deacon AM","Wilson IA."],"DOI_URL":null}},"set_info":{"accession":"CL0125","name":"Peptidase_CA"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":9,"interactions":0,"matches":1254,"pathways":0,"proteins":1249,"proteomes":1222,"sets":1,"structural_models":{"alphafold":812},"structures":5,"taxa":2039},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":13,"alignment:full":602},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4q68","name":"Crystal structure of a N-acetylmuramoyl-L-alanine amidase (BACUNI_02947) from Bacteroides uniformis ATCC 8492 at 1.07 A resolution"}}}