ID   ERG27_KLULA             Reviewed;         346 AA.
AC   Q6CJC2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=3-keto-steroid reductase;
DE            EC=1.1.1.270;
GN   Name=ERG27; OrderedLocusNames=KLLA0F19756g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98675.1; -; Genomic_DNA.
DR   RefSeq; XP_455967.1; XM_455967.1.
DR   AlphaFoldDB; Q6CJC2; -.
DR   STRING; 28985.XP_455967.1; -.
DR   EnsemblFungi; CAG98675; CAG98675; KLLA0_F19756g.
DR   GeneID; 2895502; -.
DR   KEGG; kla:KLLA0_F19756g; -.
DR   eggNOG; KOG1478; Eukaryota.
DR   HOGENOM; CLU_029944_1_0_1; -.
DR   InParanoid; Q6CJC2; -.
DR   OMA; ASYEGSK; -.
DR   UniPathway; UPA00770; UER00758.
DR   Proteomes; UP000000598; Chromosome F.
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; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
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_0000054593"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39395 MW;  7986B74A9B8920F1 CRC64;
     MSSSKVAVVT GTNSNLGLNI VYRLIERSEP EDNLTIVVTS RTLPRVRECI DLIKAFVNTI
     NRTGSVDYDY LLVDFTNMIS ILDAHYSLSK RYDHINYFFV NAAQGVYSGI DWLGAVKEVF
     SSPLEAVTNP TYKIQRVGVK SKDGMGLVFQ ANVFGPYYLI QKLLPLLQAG QGTVVWVSSI
     MSAPKYLSLQ DIQLLESDVS YEGSKRLVDL LHSATYKEMK KLGIRQYLTH PGIFTSLSFF
     QYLNVFTYYG MLFLFYLARW IGSPWHNIQG YKAANAPVYV ATMANPHFEK EQMKYGSATF
     RDGLEYIKTD EVDTTGCEDV YKYISNLKLQ WDEKLKDQIK PTRIPL