InterPro API

GET /api/protein/UniProt/Q4WR24/?format=api

HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept

{
    "metadata": {
        "accession": "Q4WR24",
        "id": "HELE_ASPFU",
        "source_organism": {
            "taxId": "330879",
            "scientificName": "Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)",
            "fullName": "Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)"
        },
        "name": "3-ketosteroid 1-dehydrogenase helE",
        "description": [
            "3-ketosteroid 1-dehydrogenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19216560, PubMed:19415934, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol) (PubMed:19216560, PubMed:19415934, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19216560, PubMed:19415934, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519)"
        ],
        "length": 596,
        "sequence": "MAARQLRRLSLPTHLPLPIRPHVRHLGTAQTNCHRFDHETDILIVGSGAAGLTAALRSHFHGLSSLVIEKDAQIGGTSAYSGGGLWIPNNPLAVEAGIIDTPEQAMTYLISVIDADTAEDTDVRRASSPPRKRAFLTHGPHMVSFLRDRGFAFRLSPGCPDYYPQAHGALPTGGRSIEPDVFDARLLGLGEKWTEAIRQRPGRSLPLFTYEASSVTRMGASWRDVGTVLRVLLRGIYLSRVRGQIPVTMGKSLVAQLLWLHMQLDQGPVLTDTALRQLIATPEGVILGARVATPDGERSIRARCGVLLCAGGFAHNQGLRERYGPVPANAEWTSAARGDNGDAIVAGVRVGAATALMDEAWWGPTLRDPVRGMYYFALQERARPFGVIVDSSGKRFMNEAEPYTDAGHHQYAQKAVPAWFVFDWNHRKRYAVGSLMPRQQPPAQALDAGYIHRADTIAELARQIGVNEKGLEGTLARFNEMADCGVDSDFARGESAFDNYFGDPTVRPNPNLGAVRTPPFYAIPLVPGDLGTKGGLLTDEHARVIREDGTPVQGLYAAGNTTASVMGRTYPGAGATLGPAMTFAFIAIDHIASEHV",
        "proteome": "UP000002530",
        "gene": "helE",
        "go_terms": null,
        "protein_evidence": 1,
        "source_database": "reviewed",
        "is_fragment": false,
        "in_alphafold": true,
        "in_bfvd": false,
        "ida_accession": "f8c050f2bae5a7641bef04066a98503b1963e30d",
        "counters": {
            "domain_architectures": 40274,
            "entries": 9,
            "isoforms": 0,
            "proteomes": 1,
            "sets": 1,
            "structures": 0,
            "taxa": 1,
            "dbEntries": {
                "ssf": 2,
                "cathgene3d": 1,
                "pfam": 1,
                "panther": 1,
                "interpro": 4
            },
            "proteome": 1,
            "taxonomy": 1,
            "similar_proteins": 40274
        }
    }
}

General Handler