ID   TSC10_DEBHA             Reviewed;         328 AA.
AC   Q6BQK1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 99.
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=DEHA2E04576g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG87745.2; -; Genomic_DNA.
DR   RefSeq; XP_459519.2; XM_459519.1.
DR   AlphaFoldDB; Q6BQK1; -.
DR   SMR; Q6BQK1; -.
DR   STRING; 4959.XP_459519.2; -.
DR   EnsemblFungi; CAG87745; CAG87745; DEHA2E04576g.
DR   GeneID; 2902161; -.
DR   KEGG; dha:DEHA2E04576g; -.
DR   VEuPathDB; FungiDB:DEHA2E04576g; -.
DR   eggNOG; KOG1210; Eukaryota.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   InParanoid; Q6BQK1; -.
DR   OMA; NCAGMAI; -.
DR   OrthoDB; 1210617at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000000599; Chromosome E.
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:0047560; F:3-dehydrosphinganine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006666; P:3-keto-sphinganine metabolic process; IEA:InterPro.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
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..328
FT                   /note="3-ketodihydrosphingosine reductase TSC10"
FT                   /id="PRO_0000054795"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          213..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
FT   BINDING         16..40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   328 AA;  36663 MW;  ED567CA13B25DC16 CRC64;
     MLFSNNKIHA EGKLALIVGA SQGLGADLAL KLYQQNCSVI LVARTETKLV AQIERIQSSS
     PENNATLSYK CCDASNYEDC VKLWNDLIVD QKQDPDFIFC CAGSSIPKLF SDLTAKDFAI
     GINTNYTTSL NITHTGFKQV LGQFSDLSCD QYKKRHVIFV SSVVSFYPFI GYSQYAPLKS
     AIQSLSIILR QEMGPFNYRV SCVFPGNFQS EGYEEEQKTK PSITKSIEGS SKPISGEDCA
     DIILNQLNRG YDTVTTDFIG WLLGCSVLGV LPRSWGFFQV IVSFIFSIIA PIANYVVYRD
     VLKFFKTRST REVEEYEIVS TDDNKKTL