ID   TSC10_YARLI             Reviewed;         372 AA.
AC   Q6CE86;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=YALI0B17688g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83279.1; -; Genomic_DNA.
DR   RefSeq; XP_501026.1; XM_501026.1.
DR   AlphaFoldDB; Q6CE86; -.
DR   SMR; Q6CE86; -.
DR   STRING; 4952.CAG83279; -.
DR   EnsemblFungi; CAG83279; CAG83279; YALI0_B17688g.
DR   GeneID; 2907213; -.
DR   KEGG; yli:YALI0B17688g; -.
DR   VEuPathDB; FungiDB:YALI0_B17688g; -.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   InParanoid; Q6CE86; -.
DR   OMA; NCAGMAI; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001300; Chromosome B.
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: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; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 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..372
FT                   /note="3-ketodihydrosphingosine reductase TSC10"
FT                   /id="PRO_0000054799"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        219
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   BINDING         64..88
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  40734 MW;  5B57E9E6E5DE0687 CRC64;
     MIFPISEIPD KVTHSILEGV SALQNMSHTA FWSTVLGFLV VARIAVILAT PKRRVLDIKG
     KKVVISGGSQ GAGAALAELC YTKGANVVIV SRTVSKLEAQ VQKIVTKHEP VFEGQTIRYI
     SADLTKEEEA IRVFSEETMP APPDVIFSCA GAAETGFILD FKASQLARAF STNYLSALFF
     VHAGTTRMAK EPISPKNPRY VAIFSSVLAF YPLLGYGQYC ASKAAVRSLI DSLRVEALPF
     NIRVVGVFPG NFQSEGFEEE NKSKPEITRQ IEGPSQAISA EECAKIVFAQ MEKGGQMITT
     DLIGWILQSI ALSSSPRSFS LLQIPLAIFM CIFSPVWNAF VNRDVRKYFH ANTEYVTRHQ
     RGGVGSENPT PQ