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TSC10_CRYNB
ID   TSC10_CRYNB             Reviewed;         335 AA.
AC   P0CR37; Q55NW2; Q5KEJ9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
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=CNBG4500;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000039; EAL19503.1; -; Genomic_DNA.
DR   RefSeq; XP_774150.1; XM_769057.1.
DR   AlphaFoldDB; P0CR37; -.
DR   SMR; P0CR37; -.
DR   EnsemblFungi; EAL19503; EAL19503; CNBG4500.
DR   GeneID; 4937486; -.
DR   KEGG; cnb:CNBG4500; -.
DR   VEuPathDB; FungiDB:CNBG4500; -.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001435; Chromosome 7.
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   Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..335
FT                   /note="3-ketodihydrosphingosine reductase TSC10"
FT                   /id="PRO_0000410280"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000250"
FT   BINDING         7..28
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  36504 MW;  B59B87DA86C92D40 CRC64;
     MPTPLALLLS AILIIGTYFA MPFWPFRKSN YDPRGKHCYI TGGSSGLGKA LAERLVKQGA
     HVTIVGRDSK KAEGVVEELK AIAAPGQIIQ CIAADLTSPI ASTNAIHAAC KPHADQAPDY
     VYLCAGFSRP KLFVETTKQE LKDGLDGVYW VSAYTAHEAC QMMSKQRRTG KIIFVASFLS
     YVSFAGYSSY SPAKYALRGL SDALRSEMLL HNIDIHIFLP CGISGPGFDA ENRTKPAVTK
     KIEEGDTPIT PEVCAAALES GLKKGYYQIT DNLVTEPIRL RSNGGVPTNN FLLDTLWLIV
     SSVGVPIWRM TADSAVRSFR AKVEKELEAK GYYVS
 
 
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