{"metadata":{"accession":"PF11927","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021848","hierarchy":null,"name":{"name":"Haem-dependent oxidative N-demethylase, alpha subunit-like","short":"HODM_asu-like"},"description":[{"text":"<p>This protein family is found in fungi and bacteria, including the alpha subunit of an haem-dependent oxidative N-demethylase (HODM) from Pseudomonas mendocina. This protein, catalytically active, is responsible for haem, oxygen and NADPH-dependent dimethylamine (DMA) binding. It shows structural similarity to the to the Aer2 PAS domain, but lacks the core PAS-domain alpha-helix that forms the Aer2 haem pocket, and displays extended beta-strands and a longer loop [[cite:PUB00100877]]. The structure of [swissprot:A4XXY9], PDBe:5lte, shows that it is an haem-binding PAS domain, similar in structure to PAS gas sensors [[cite:PUB00100877]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100877":{"PMID":27851736,"ISBN":null,"volume":"539","issue":"7630","year":2016,"title":"An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.","URL":null,"raw_pages":"593-597","medline_journal":"Nature","ISO_journal":"Nature","authors":["Ortmayer M","Lafite P","Menon BR","Tralau T","Fisher K","Denkhaus L","Scrutton NS","Rigby SE","Munro AW","Hay S","Leys D."],"DOI_URL":null}},"set_info":{"accession":"CL0183","name":"PAS_Fold"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":88,"interactions":0,"matches":6341,"pathways":0,"proteins":6200,"proteomes":3026,"sets":1,"structural_models":{"alphafold":4748},"structures":3,"taxa":5492},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":210,"alignment:full":4566},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"5lte","name":"Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM)"}}}