{"metadata":{"accession":"PF08982","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR015075","hierarchy":null,"name":{"name":"Acetylaranotin biosynthesis cluster protein L","short":"AtaL"},"description":[{"text":"<p>This entry includes acetylaranotin biosynthesis cluster protein L (AtaL) from Aspergillus terreus, which is a non-ribosomal peptide synthetase. It is required for the biosynthesis of the toxin acetylaranotin, which is a disulfide bridged cyclic dipeptide [[cite:PUB00086035]]. There are a number of steps in the biosyntheis of this epipolythiodioxopiperazine toxin from two phenylananines, but the specific function of AtaL has yet to be determined [[cite:PUB00086035]]. Homologues are also known from bacteria.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00086035":{"PMID":23586797,"ISBN":null,"volume":"135","issue":"19","year":2013,"title":"Biosynthetic pathway for the epipolythiodioxopiperazine acetylaranotin in Aspergillus terreus revealed by genome-based deletion analysis.","URL":null,"raw_pages":"7205-13","medline_journal":"J Am Chem Soc","ISO_journal":"J. Am. Chem. Soc.","authors":["Guo CJ","Yeh HH","Chiang YM","Sanchez JF","Chang SL","Bruno KS","Wang CC."],"DOI_URL":"https://doi.org/10.1021/ja3123653"}},"set_info":{"accession":"CL0209","name":"Bet_v_1_like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":27,"interactions":0,"matches":1822,"pathways":0,"proteins":1820,"proteomes":1519,"sets":1,"structural_models":{"alphafold":1347},"structures":1,"taxa":2674},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":64,"alignment:full":1184},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}