ID   ERG27_CANGA             Reviewed;         348 AA.
AC   Q6FIV3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=3-keto-steroid reductase;
DE            EC=1.1.1.270;
GN   Name=ERG27; OrderedLocusNames=CAGL0M11506g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62821.1; -; Genomic_DNA.
DR   RefSeq; XP_449841.1; XM_449841.1.
DR   AlphaFoldDB; Q6FIV3; -.
DR   SMR; Q6FIV3; -.
DR   STRING; 5478.XP_449841.1; -.
DR   EnsemblFungi; CAG62821; CAG62821; CAGL0M11506g.
DR   GeneID; 2891410; -.
DR   KEGG; cgr:CAGL0M11506g; -.
DR   CGD; CAL0136807; CAGL0M11506g.
DR   VEuPathDB; FungiDB:CAGL0M11506g; -.
DR   eggNOG; KOG1478; Eukaryota.
DR   HOGENOM; CLU_029944_1_0_1; -.
DR   InParanoid; Q6FIV3; -.
DR   OMA; ASYEGSK; -.
DR   UniPathway; UPA00770; UER00758.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
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:0006696; P:ergosterol biosynthetic process; IEA:EnsemblFungi.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis.
FT   CHAIN           1..348
FT                   /note="3-keto-steroid reductase"
FT                   /id="PRO_0000054591"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  39505 MW;  5636A881CD1F7645 CRC64;
     MTSKTRKVAV ITGANSNLGL NIAYRLIERQ SADVRLTLVV TSRTLPRVRE VVELIKKFVA
     TQEDPCSVDF DYLLVDFTNM VSVLNAYYDL NQKYESINYF FVNAAQGVYD GIDWIGAVKQ
     VLSDPLEAVT NPTYRKQLVG VKSKDEMGLV FQANVFGPYY LIQKILPQLS KGKATVVWIS
     SIMADPKHLS LQDIEMIKSD VTYEGSKRVV DLLHLATYKQ MKSQGIHQYV VQPGIFTSYS
     FAKYLNFFTT FGMLFLFYLA RLLGSKWHNI DGYKAANAPV YVATLINPHF EHQEVKYGSA
     SSRDGMEYIE TTDIDKTGSS DVLAYIEKKK LEWDDKLKDQ ITNSRIPI