TSC10_CRYNJ
ID TSC10_CRYNJ Reviewed; 335 AA.
AC P0CR36; Q55NW2; Q5KEJ9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=CNG00270;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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; AE017347; AAW44453.1; -; Genomic_DNA.
DR RefSeq; XP_571760.1; XM_571760.1.
DR AlphaFoldDB; P0CR36; -.
DR SMR; P0CR36; -.
DR STRING; 5207.AAW44453; -.
DR PaxDb; P0CR36; -.
DR EnsemblFungi; AAW44453; AAW44453; CNG00270.
DR GeneID; 3258921; -.
DR KEGG; cne:CNG00270; -.
DR VEuPathDB; FungiDB:CNG00270; -.
DR eggNOG; KOG1210; Eukaryota.
DR HOGENOM; CLU_010194_3_0_1; -.
DR InParanoid; P0CR36; -.
DR OMA; PFIGYGQ; -.
DR OrthoDB; 1210617at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000002149; Chromosome 7.
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; 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..335
FT /note="3-ketodihydrosphingosine reductase TSC10"
FT /id="PRO_0000054794"
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; 36490 MW; 548A87DB5C625C9A 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 PDVCAAALES GLKKGYYQIT DNLVTEPIRL RSNGGVPTNN FLLDTLWLIV
SSVGVPIWRM TADSAVRSFR AKVEKELEAK GYYVS
