GET /api/protein/UniProt/Q3S2U2/?format=api
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InterPro-Version: 108.0
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{
    "metadata": {
        "accession": "Q3S2U2",
        "id": "MOKF_MONPI",
        "source_organism": {
            "taxId": "89488",
            "scientificName": "Monascus pilosus",
            "fullName": "Monascus pilosus (Red mold)"
        },
        "name": "Acyltransferase mokF",
        "description": [
            "Acyltransferase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535, PubMed:19693441). MokF catalyzes the last step of the pathway by adding the side-chain (2R)-2-methylbutanoate produced by the diketide synthase mokB onto monacoline J to yield monacoline K (By similarity). Monakolin K biosynthesis is performed in two stages. The first stage is catalyzed by the nonaketide synthase mokA with the help of the enoyl reductase mokE that catalyze the iterative nine-step formation that leads to the formation of dihydromonacolin L. Covalently bound dihydromonacolin L is released from mokA by the mokD esterase. Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC. Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (Probable)"
        ],
        "length": 413,
        "sequence": "MRQFLSSDRINSEIPQEKSEMVGFSDIDNSSRQIKEMEAAFRSAVKTGQIPGAVIMARDHSGRLNYTRCFGARTVVRDECNRLPPMQVDTPCRLASATKLLTTIMALQCVERGLVRLDETVDRLLPDLSAMKVLEGFDAAGEPKMRERKGKITLKHLLTHTSGLSYVFLHPLLREYMAKGHLQTAEKFGIQSRLAPPAVNDPGAEWIYGANLDWTGKLVERATGLDLEQYLQENICAPLNITDMTFKLQQRPDLLARRADQTHRNKADGRLRYDDSVYFRSDGDECFGGQGVFSGPESYMKVVHSLLQRDGRLLRPETVDLMFQPALDAQTEKQMNQHMDASPHINYGGPMPMVLRRSFGLGGMIALEDLDGQKWRRKGCLTFGGGPNIVWVMLLSALRFVFFFFFFFFFCSS",
        "proteome": null,
        "gene": "mokF",
        "go_terms": null,
        "protein_evidence": 1,
        "source_database": "reviewed",
        "is_fragment": false,
        "in_alphafold": true,
        "in_bfvd": false,
        "ida_accession": "6eccaef758bed472747734f6b0565810a6ecc3b1",
        "counters": {
            "domain_architectures": 128765,
            "entries": 7,
            "isoforms": 0,
            "proteomes": 0,
            "sets": 1,
            "structures": 0,
            "taxa": 1,
            "dbEntries": {
                "cathgene3d": 1,
                "ssf": 1,
                "pfam": 1,
                "panther": 1,
                "interpro": 3
            },
            "proteome": 0,
            "taxonomy": 1,
            "similar_proteins": 128765
        }
    }
}