ID   ERG27_YARLI             Reviewed;         343 AA.
AC   Q6CE88;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=3-keto-steroid reductase;
DE            EC=1.1.1.270;
GN   Name=ERG27; OrderedLocusNames=YALI0B17644g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Responsible for the reduction of the keto group on the C-3 of
CC       sterols. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC         NADPH; Xref=Rhea:RHEA:34787, ChEBI:CHEBI:15378, ChEBI:CHEBI:36836,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.270;
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 5/6.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. ERG27 subfamily. {ECO:0000305}.
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DR   EMBL; CR382128; CAG83277.1; -; Genomic_DNA.
DR   RefSeq; XP_501024.1; XM_501024.1.
DR   AlphaFoldDB; Q6CE88; -.
DR   SMR; Q6CE88; -.
DR   STRING; 4952.CAG83277; -.
DR   EnsemblFungi; CAG83277; CAG83277; YALI0_B17644g.
DR   GeneID; 2907211; -.
DR   KEGG; yli:YALI0B17644g; -.
DR   VEuPathDB; FungiDB:YALI0_B17644g; -.
DR   HOGENOM; CLU_029944_1_0_1; -.
DR   InParanoid; Q6CE88; -.
DR   OMA; ASYEGSK; -.
DR   UniPathway; UPA00770; UER00758.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR   GO; GO:0000253; F:3-keto sterol reductase activity; IBA:GO_Central.
DR   GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis.
FT   CHAIN           1..343
FT                   /note="3-keto-steroid reductase"
FT                   /id="PRO_0000054594"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  38724 MW;  A6A0233F4A782283 CRC64;
     MIHNRKTQTV VITGASSNLG IAIGKRLIDE KKEDAHLTIV VTSRTLRNVR VAIKTLKAHA
     VAKEVGPEVD FDYLLFDLAD MTSINGALVE LKLRFSRIDT LIFNSNAANY IGINWPLAMW
     RFTTQFKSEI ENPSCMIQAV GVKSDDGMGS AYQSNVFGPW YMVLELTEQL KNGGKVIWIS
     SITSSEKYVD LEDIELIHNK EPYKGSKRLI DVAHNYYSPK LEEEHGIYSY LTDPGIFTSS
     SASEYLNIFS AFGMYLMFYF ARLIGLTTMN IDPYKGANVP VWVTLSEDPS ALKREYRLGS
     RTGRWGTEMM DATKLQYEGS EEVGAYIDKG VGEWREKLKD QIN