ID   TSC10_CANGA             Reviewed;         363 AA.
AC   Q6FQ42;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=CAGL0I09328g;
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: 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}.
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; CR380955; CAG60589.1; -; Genomic_DNA.
DR   RefSeq; XP_447652.1; XM_447652.1.
DR   AlphaFoldDB; Q6FQ42; -.
DR   SMR; Q6FQ42; -.
DR   STRING; 5478.XP_447652.1; -.
DR   EnsemblFungi; CAG60589; CAG60589; CAGL0I09328g.
DR   GeneID; 2889126; -.
DR   KEGG; cgr:CAGL0I09328g; -.
DR   CGD; CAL0129687; CAGL0I09328g.
DR   VEuPathDB; FungiDB:CAGL0I09328g; -.
DR   eggNOG; KOG1210; Eukaryota.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   InParanoid; Q6FQ42; -.
DR   OMA; GHECADL; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000002428; Chromosome I.
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..363
FT                   /note="3-ketodihydrosphingosine reductase TSC10"
FT                   /id="PRO_0000054793"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000250"
FT   BINDING         10..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  40410 MW;  8AAA5C934888C4F2 CRC64;
     MFCLEDQVVL IAGGSQGLGK QFGQKYWDES RHSKIILVSR SDVKLRNAIT DITGGRQEPV
     ELVMPEVAAS EPSASGSSAI NLSKSSNHAG FESELRSNSN RSSSSLKEST NVVTHLTTNA
     ADSRIVYIAC DLSDPDAVER MFVTLQHNNL LPTQVLACAG GSIPKLFTDL TAKELEMGVK
     MNYMTTLFVI HKAAQMVPQA HLILFSSSTA FFPFIGYSQY APAKVSLKAL TSILRHELPN
     TRISCVYPGN FYSEGYVLEE MSKPDITKSI EGSSYPISCE ECCDKIVWWL NRGYDDVTTD
     SIGWFLMSLD MGLNKHNNNS AYWFVQWLIG VIANLLVVPF YMVLCSYQIN KWHKQNKNKN
     TLL