ID   TSC10_CANAL             Reviewed;         310 AA.
AC   Q59RQ2; A0A1D8PTG8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 103.
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=KSR1; Synonyms=TSC10; OrderedLocusNames=CAALFM_CR07380CA;
GN   ORFNames=CaO19.13550, CaO19.6131;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW31433.1; -; Genomic_DNA.
DR   RefSeq; XP_712338.2; XM_707245.2.
DR   AlphaFoldDB; Q59RQ2; -.
DR   SMR; Q59RQ2; -.
DR   STRING; 237561.Q59RQ2; -.
DR   PRIDE; Q59RQ2; -.
DR   GeneID; 3646052; -.
DR   KEGG; cal:CAALFM_CR07380CA; -.
DR   CGD; CAL0000189000; KSR1.
DR   VEuPathDB; FungiDB:CR_07380C_A; -.
DR   eggNOG; KOG1210; Eukaryota.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   InParanoid; Q59RQ2; -.
DR   OrthoDB; 1210617at2759; -.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:Q59RQ2; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006666; P:3-keto-sphinganine metabolic process; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
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..310
FT                   /note="3-ketodihydrosphingosine reductase TSC10"
FT                   /id="PRO_0000054792"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250"
FT   BINDING         16..40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34926 MW;  DA83340B3EB1B6F4 CRC64;
     MWFSKTNFPV EGKTALIVGA SQGIGVNLAE RLYEKNCSTI LVARTESKLQ HQIQNIKEKY
     PESSAKISYA VADVSNYDEC TRLWRTIDPA DPDILFCCAG SSIPKLFQDL TKVDIESGID
     INYKTVINVV HTGFKHALSN NTDNLEPHNF KKRSVVLFSS VVSFFPFIGY SQYAPMKSAI
     ESLSIILRQE LSPYNYRVTC VFPGNFQSEG FEEEQKTKPD ITKKIEGPSN PIPGDECARL
     IIDQLDKGYD SITTDFIGWF LGCSVLGISS PRQWGFFQIL VSFIVSLIAP IANWFINRDI
     KNSFKKTKKE