{"metadata":{"accession":"PF08354","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR013565","hierarchy":null,"name":{"name":"Fatty acid synthase subunit beta/Fas1-like, helical","short":"Fas1-AflB-like_hel"},"description":[{"text":"<p>This domain has been identified in fungi and bacteria. It is found in fatty acid synthase beta subunit from fungi, including Fas1 from yeasts and aflB from Aspergillus parasiticus. This is an inserted helical domain, whose function is not clear, and is found together with the MaoC-like domain ([pfam:PF01575]) and the acyltransferase domain ([pfam:PF00698]) [[cite:PUB00016843]]. Fas1 is a fatty acid synthetase that catalyses the formation of long-chain fatty acids from  acetyl-CoA, malonyl-CoA and NADPH [[cite:PUB00006544]]. AflB is part of the gene cluster that mediates the biosynthesis of aflatoxins [[cite:PUB00083132]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00006544":{"PMID":3528750,"ISBN":null,"volume":"203","issue":"3","year":1986,"title":"The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains.","URL":null,"raw_pages":"479-86","medline_journal":"Mol Gen Genet","ISO_journal":"Mol. Gen. Genet.","authors":["Schweizer M","Roberts LM","Holtke HJ","Takabayashi K","Hollerer E","Hoffmann B","Muller G","Kottig H","Schweizer E."],"DOI_URL":"http://dx.doi.org/10.1007/BF00422073"},"PUB00083132":{"PMID":15006741,"ISBN":null,"volume":"70","issue":"3","year":2004,"title":"Clustered pathway genes in aflatoxin biosynthesis.","URL":null,"raw_pages":"1253-62","medline_journal":"Appl Environ Microbiol","ISO_journal":"Appl. Environ. Microbiol.","authors":["Yu J","Chang PK","Ehrlich KC","Cary JW","Bhatnagar D","Cleveland TE","Payne GA","Linz JE","Woloshuk CP","Bennett JW."],"DOI_URL":"http://dx.doi.org/10.1128/AEM.70.3.1253-1262.2004"},"PUB00016843":{"PMID":9693066,"ISBN":null,"volume":"13","issue":"3","year":1998,"title":"Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex.","URL":null,"raw_pages":"403-13","medline_journal":"Protein Expr Purif","ISO_journal":"Protein Expr. Purif.","authors":["Niwa H","Katayama E","Yanagida M","Morikawa K."],"DOI_URL":"http://dx.doi.org/10.1006/prep.1998.0914"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":233,"interactions":0,"matches":3333,"pathways":0,"proteins":3260,"proteomes":2302,"sets":0,"structural_models":{"alphafold":205},"structures":45,"taxa":4165},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":8,"alignment:full":2323},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}