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Database: UniProt
Entry: E9B3N0_LEIMU
LinkDB: E9B3N0_LEIMU
Original site: E9B3N0_LEIMU 
ID   E9B3N0_LEIMU            Unreviewed;       349 AA.
AC   E9B3N0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Putative d-xylulose reductase {ECO:0000313|EMBL:CBZ29847.1};
DE            EC=1.1.1.19 {ECO:0000313|EMBL:CBZ29847.1};
GN   ORFNames=LMXM_32_0520 {ECO:0000313|EMBL:CBZ29847.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ29847.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|EMBL:CBZ29847.1, ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29847.1,
RC   ECO:0000313|Proteomes:UP000007259};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; FR799585; CBZ29847.1; -; Genomic_DNA.
DR   RefSeq; XP_003878297.1; XM_003878248.1.
DR   AlphaFoldDB; E9B3N0; -.
DR   GeneID; 13453816; -.
DR   KEGG; lmi:LMXM_32_0520; -.
DR   VEuPathDB; TriTrypDB:LmxM.32.0520; -.
DR   OMA; LKGVFHN; -.
DR   OrthoDB; 3017546at2759; -.
DR   PhylomeDB; E9B3N0; -.
DR   Proteomes; UP000007259; Chromosome 32.
DR   GO; GO:0047939; F:L-glucuronate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05285; sorbitol_DH; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR045306; SDH-like.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CBZ29847.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          13..345
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   349 AA;  37320 MW;  6A25A301E2F1C7CD CRC64;
     MVLMQSLVLE KKGELTIREV DVCDELGPHD CRVKIHSVGI CGSDVHYYEH GHIGPFVVEK
     PMILGHEASG TVVAVGAEVK NLKTGDRVAL EPGIPRWNSA QTLTGLYNLD PELTFFATPP
     VHGCMSTTII HPAALCFKLP DNVSYEEGAL CEPVAVGMHS ATKAGIKPGD VGLVIGCGTI
     GIVTALSALA GGCSEVIICG SRDERLEIAG RYPGLRAVNT SREGELQCAV AEATEGNGCD
     VVFECGGAAS AFPLIYENAA PGATCVLVGM PVEPVPVDIV MAQAKEITFQ TAFRYRNVYP
     RIIRLLSSGK MDVKPLISAK FAFKDSVKAY ERAMNRDPKD MKIMIQMES
//
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