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{
"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
}
}
