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Database: UniProt
Entry: G0UW10_TRYCI
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Original site: G0UW10_TRYCI 
ID   G0UW10_TRYCI            Unreviewed;       347 AA.
AC   G0UW10;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=3-dehydrosphinganine reductase {ECO:0000256|ARBA:ARBA00026112};
DE            EC=1.1.1.102 {ECO:0000256|ARBA:ARBA00026112};
GN   ORFNames=TCIL3000_10_3370 {ECO:0000313|EMBL:CCC93576.1};
OS   Trypanosoma congolense (strain IL3000).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC93576.1};
RN   [1] {ECO:0000313|EMBL:CCC93576.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IL3000 {ECO:0000313|EMBL:CCC93576.1};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA   Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA   Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA   Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT   African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|RuleBase:RU000363}.
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DR   EMBL; HE575323; CCC93576.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0UW10; -.
DR   VEuPathDB; TriTrypDB:TcIL3000_10_3370; -.
DR   OrthoDB; 7812at2759; -.
DR   GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IEA:InterPro.
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   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   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
SQ   SEQUENCE   347 AA;  37974 MW;  0C063CC80D2E47FF CRC64;
     MIICTVCAAL FGVIVVAVWW SVHRVPLFPI NGCCALVTGG SLGIGLETAR ELVRRGARLV
     IIAARNEETL KTAVEELRTE VVGRDTKVEY VVMDVADETS VSRALEEVMR TLQTTGKAAL
     DLVVCNAGFS VPSRFVDITP AEGRRMMDVN FFGCVNVVRA VLPSMLQQRG GRFVFVSSLA
     ARCPLAGYSI YAASKAAIRA FAHSLDMENS YKGVRCQVIS PPDVYTPGLE QENLRKSPEC
     SALSSFGGDA PVTAADMGRR VTNSIVNYRF DESIGFDKQL LCWAVAGTEP ATGVLELFMQ
     FLFSGWLRLF LAVLSKLHYN IVLRVRVDEE KKKKPEPVGT GQLKKNL
//
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