ID   TSC10_KLULA             Reviewed;         313 AA.
AC   Q6CLN0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=3-ketodihydrosphingosine reductase TSC10;
DE            EC=1.1.1.102;
DE   AltName: Full=3-dehydrosphinganine reductase;
DE   AltName: Full=KDS reductase;
GN   Name=TSC10; OrderedLocusNames=KLLA0F01749g;
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: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC       dihydrosphingosine (DHS). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH;
CC         Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349;
CC         EC=1.1.1.102;
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CR382126; CAG97866.1; -; Genomic_DNA.
DR   RefSeq; XP_455159.1; XM_455159.1.
DR   AlphaFoldDB; Q6CLN0; -.
DR   SMR; Q6CLN0; -.
DR   STRING; 28985.XP_455159.1; -.
DR   PRIDE; Q6CLN0; -.
DR   EnsemblFungi; CAG97866; CAG97866; KLLA0_F01749g.
DR   GeneID; 2895346; -.
DR   KEGG; kla:KLLA0_F01749g; -.
DR   eggNOG; KOG1210; Eukaryota.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   InParanoid; Q6CLN0; -.
DR   OMA; GAHPNEP; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006666; P:3-keto-sphinganine metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:EnsemblFungi.
DR   CDD; cd08939; KDSR-like_SDR_c; 1.
DR   InterPro; IPR045022; KDSR-like.
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   Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome; Sphingolipid metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..313
FT                   /note="3-ketodihydrosphingosine reductase TSC10"
FT                   /id="PRO_0000054797"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   BINDING         12..43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  34859 MW;  50FA51DEF578E080 CRC64;
     MKGFNCNGQV ILISGGSQGL GESFAKRFVQ DDDGPGSNTN KVIIVSRSQS KLVKACERIG
     VDGVSLDRYV NDTNRNETKL IYHSCDTSSY DKVALMFKLL VKSELVPSQV YMCAGGSIPK
     LFLDLTPEEL QNGITTNYST AVNLAHVSLK HDVPHLLFFS SEVAFFPFIG YAQYAPLKQS
     IRSLVAILRQ EHSSTRITCV YPGNFQSEGF DLENITKPAI TKEIEGPSNP VTAAQCRDKI
     ISSLKWGLDD ITTDSIGWLL MACDQGLNKH STSQFMFVFS WILGALLNIT IVPIYMLICK
     FQIYQWKRNK DTK