{"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}}}