ID   ERG27_DEBHA             Reviewed;         346 AA.
AC   Q6BNP0;
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=DEHA2E20130g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382137; CAG88453.1; -; Genomic_DNA.
DR   RefSeq; XP_460180.1; XM_460180.1.
DR   AlphaFoldDB; Q6BNP0; -.
DR   SMR; Q6BNP0; -.
DR   STRING; 4959.XP_460180.1; -.
DR   EnsemblFungi; CAG88453; CAG88453; DEHA2E20130g.
DR   GeneID; 2902497; -.
DR   KEGG; dha:DEHA2E20130g; -.
DR   VEuPathDB; FungiDB:DEHA2E20130g; -.
DR   eggNOG; KOG1478; Eukaryota.
DR   HOGENOM; CLU_029944_1_0_1; -.
DR   InParanoid; Q6BNP0; -.
DR   OMA; ASYEGSK; -.
DR   OrthoDB; 1413827at2759; -.
DR   UniPathway; UPA00770; UER00758.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0000253; F:3-keto sterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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..346
FT                   /note="3-keto-steroid reductase"
FT                   /id="PRO_0000054592"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39154 MW;  15F6E90AA1EB0BB1 CRC64;
     MIKDNDNSKV ALITGTSSNL GINIAYRLLE QLPSSTNVTL IVTSRTLPKV KEVITNINQY
     SKTKLNRTGQ LEFDYLLVDF TDMVSVLSAY YDLNKKFKKI DYLFVNAAQG VYSGIDWVAA
     TKEICRNPME GVTNPTYKTQ RVGVKSNDNM GLVFQANVFG PYYLIHKIKH LLQKGGRIIW
     ISSLMSNPKY LSFNDLQLLK SPESYEGSKR LVDLMHFGTF KQLQSEYGIE QYLVQPGIFT
     SFSFFKFLNV FTYYSMLMLF YLARLFGSPS HNISGFIAAN APVTCALGNE SQSVKVCSVS
     NRTGKEYLSY QEVDTTGSAD ISAYLEKLCH EWDLTLKDQI VNTRQP