ID C5MAH7_CANTT Unreviewed; 308 AA.
AC C5MAH7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=3-ketodihydrosphingosine reductase TSC10 {ECO:0000256|ARBA:ARBA00026241};
DE EC=1.1.1.102 {ECO:0000256|ARBA:ARBA00026112};
DE AltName: Full=3-dehydrosphinganine reductase {ECO:0000256|ARBA:ARBA00032891};
DE AltName: Full=KDS reductase {ECO:0000256|ARBA:ARBA00029797};
GN ORFNames=CTRG_03069 {ECO:0000313|EMBL:EER32644.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32644.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER32644.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC dihydrosphingosine (DHS). {ECO:0000256|ARBA:ARBA00025686}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; GG692398; EER32644.1; -; Genomic_DNA.
DR RefSeq; XP_002548772.1; XM_002548726.1.
DR AlphaFoldDB; C5MAH7; -.
DR STRING; 294747.C5MAH7; -.
DR EnsemblFungi; CTRG_03069-t43_1; CTRG_03069-t43_1-p1; CTRG_03069.
DR GeneID; 8297683; -.
DR KEGG; ctp:CTRG_03069; -.
DR VEuPathDB; FungiDB:CTRG_03069; -.
DR eggNOG; KOG1210; Eukaryota.
DR HOGENOM; CLU_010194_3_0_1; -.
DR OrthoDB; 316379at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IEA:EnsemblFungi.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045022; KDSR-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43550; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 1.
DR PANTHER; PTHR43550:SF3; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 153..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 308 AA; 34701 MW; C36F23270AD0A60A CRC64;
MWFSKSNFPI EGKTAIIIGA SQGVGADIAS KLYSKNCSVI LVARTESKLQ QQVSRIKKEH
SKSTAKISYS VADVSKYEEC VNLWNSIYPI DPDIIFCCAG SSIPKLFQDL TERDINSGID
INYKTAINIA HTGFKHVLEK HSNKDHEFKK RHIILFSSVV SFFPFIGYSQ YAPMKSALES
LSIILRQELS PYNYRVSCVF PGNFQSEGFE EEQKTKPEIT KKIEGPSNPI PGDECAEMII
DQLSKGYDTI TTDFVGWVLG TTSLGVFLPR QWGFFQVIIG FFISLIGPIV NWVINRDIQN
SIDKKKKE
//
