TSC10_ASHGO
ID TSC10_ASHGO Reviewed; 307 AA.
AC Q758B6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=AEL164C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016818; AAS52521.1; -; Genomic_DNA.
DR RefSeq; NP_984697.1; NM_210050.1.
DR AlphaFoldDB; Q758B6; -.
DR SMR; Q758B6; -.
DR STRING; 33169.AAS52521; -.
DR EnsemblFungi; AAS52521; AAS52521; AGOS_AEL164C.
DR GeneID; 4620882; -.
DR KEGG; ago:AGOS_AEL164C; -.
DR eggNOG; KOG1210; Eukaryota.
DR HOGENOM; CLU_010194_3_0_1; -.
DR InParanoid; Q758B6; -.
DR OMA; PFIGYGQ; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000591; Chromosome V.
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..307
FT /note="3-ketodihydrosphingosine reductase TSC10"
FT /id="PRO_0000054791"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT BINDING 11..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 307 AA; 32760 MW; 02F0E8EDF6AF8CD0 CRC64;
MKYELNGQVV LISGGSQGLG RAFAQKYIEE SDSTVVIVSR SEEKLTRAGE AICGGARRLG
AGGAGRLLYY ACNLGDAAAV GGLFATLADA GLQVTQVLFC AGGAVPGLFA ELSSAQLAAG
VEMNYGTALH LAHGAVRHGA RHLVFFSSAA AVYPFIGYSQ YAPLKAALRA LVAVLRQECD
GVRVSCVYPG NFASEGYAEE NRTKPAITAA IEGSSEAISC AACCDKIVRG LRSGYDDVTT
DFVGWLLLAC NMGFNYHSTT YFLWPLGWLL GALVNLLVVP IYMLLCRWDI HKWRTQREET
HLAAKTD