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{
    "metadata": {
        "accession": "F5HN72",
        "id": "CPAO_ASPOZ",
        "source_organism": {
            "taxId": "5062",
            "scientificName": "Aspergillus oryzae",
            "fullName": "Aspergillus oryzae (Yellow koji mold)"
        },
        "name": "Beta-cyclopiazonate dehydrogenase",
        "description": [
            "Beta-cyclopiazonate dehydrogenase; part of the gene cluster that mediates the biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole tetramic acid scaffold (PubMed:21608094). The hybrid two module polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) cpaS incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway. CpaS catalyzes a Dieckmann-type cyclization on the N-acetoacetyl-Trp intermediate bound in thioester linkage to the phosphopantetheinyl arm of the T domain to form and release c-AATrp (PubMed:19663400). CpaD then regiospecifically dimethylallylates c-AATrp to form beta-cyclopiazonic acid. CpaD discriminates against free Trp but accepts tryptophan-containing thiohydantoins, diketopiperazines, and linear peptides as substrates for C4-prenylation and also acts as regiospecific O-dimethylallyltransferase (DMAT) on a tyrosine-derived tetramic acid (PubMed:19877600, PubMed:21608094). The beta-cyclopiazonate dehydrogenase cpaO then carries out the dehydrogenation of beta-CPA to yield an unstable enimine product, which is captured by intramolecular cyclization to create the pentacyclic fused scaffold of alpha-cyclopiazonate (PubMed:21608094). Finally, the cytochrome P450 monooxygenase cpaH mediates the conversion of CPA into the less toxic 2-oxocyclopiazonic acid, the end product of the CPA pathway in A.oryza (PubMed:21608094)"
        ],
        "length": 455,
        "sequence": "MAVRIARFLGLSTVAYLALANGIDARDTISRDVIILGGGSSGTYAAIRLRDQGKTVAVVERNNYLGGHGETYYTEDNTPLNFGVEGFFNTTVTRNYLERLQVPYGRRDPAPAHEDYVNLNTGQRTEYTPGQLQDREAFAKWVDAISQFGFLDDGVYRIPEPVPEDLISPFADFVKKYHLEDAVYALFSHTSGDVLEMITLYVIQYIGVPHAAALNEGYVRPIEGIAALYKSAGKELGSDVLLETTPEAVQRFEDGVEVIVRSADGTKTLLKGKQLLVTIPPLLENLHGFPLSDQESRLFSKWQYHQYWAALVNDTGLPDDVNIVNVDTERLYGVPEEPFIWRLDNHWAPGYHNIKLVGGSEFGEDEAKAYMYERLDLLHAEGTYATHKPEIVKFASHTPVTMFVSAEEIRGGFYRQLYELQGLNSTFWTGATWASDYSTLLWGYTDEVLDQMASS",
        "proteome": null,
        "gene": "cpaO",
        "go_terms": [
            {
                "identifier": "GO:0016491",
                "name": "oxidoreductase activity",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            }
        ],
        "protein_evidence": 1,
        "source_database": "reviewed",
        "is_fragment": false,
        "in_alphafold": true,
        "in_bfvd": false,
        "ida_accession": "5b5f43762a8111a79c1821931049e93de119ed5a",
        "counters": {
            "domain_architectures": 114707,
            "entries": 7,
            "isoforms": 0,
            "proteomes": 0,
            "sets": 1,
            "structures": 0,
            "taxa": 1,
            "dbEntries": {
                "ssf": 1,
                "cathgene3d": 3,
                "pfam": 1,
                "interpro": 2
            },
            "proteome": 0,
            "taxonomy": 1,
            "similar_proteins": 114707
        }
    }
}