{"metadata":{"accession":"PF01565","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR006094","hierarchy":null,"name":{"name":"FAD binding domain","short":"FAD_binding_4"},"description":[{"text":"<p>This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [[cite:PUB00005295]]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme [ec:1.1.1.158].  This enzyme is involved in the biosynthesis of peptidoglycan [[cite:PUB00007935]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00007935":{"PMID":8805513,"ISBN":null,"volume":"4","issue":"1","year":1996,"title":"The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.","URL":null,"raw_pages":"47-54","medline_journal":"Structure","ISO_journal":"Structure","authors":["Benson TE","Walsh CT","Hogle JM."],"DOI_URL":"http://dx.doi.org/10.1016/S0969-2126(96)00008-1"},"PUB00005295":{"PMID":9261083,"ISBN":null,"volume":"5","issue":"7","year":1997,"title":"Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.","URL":null,"raw_pages":"907-20","medline_journal":"Structure","ISO_journal":"Structure","authors":["Mattevi A","Fraaije MW","Mozzarelli A","Olivi L","Coda A","van Berkel WJ."],"DOI_URL":"http://dx.doi.org/10.1016/S0969-2126(97)00245-1"}},"set_info":{"accession":"CL0077","name":"FAD_PCMH"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1520,"interactions":0,"matches":212500,"pathways":0,"proteins":211607,"proteomes":20823,"sets":1,"structural_models":{"alphafold":164681,"bfvd":12},"structures":266,"taxa":39606},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":115,"alignment:full":99587},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}