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
//