ID   XYLD_MORMO              Reviewed;         338 AA.
AC   Q59545;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=D-xylulose reductase;
DE            EC=1.1.1.9;
DE   AltName: Full=Xylitol dehydrogenase;
DE            Short=XDH;
OS   Morganella morganii (Proteus morganii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25829 / DSM 6675 / NCTC 417 / M4;
RA   Gallo M.A., Mortlock R.P.;
RT   "Molecular characterization of xylitol catabolic pathways in the
RT   Enterobacteriaceae.";
RL   Thesis (1991), University of Wisconsin-Madison, United States.
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 25829 / DSM 6675 / NCTC 417 / M4;
RX   PubMed=3886639; DOI=10.1128/jb.162.2.845-848.1985;
RA   Doten R.C., Mortlock R.P.;
RT   "Inducible xylitol dehydrogenases in enteric bacteria.";
RL   J. Bacteriol. 162:845-848(1985).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC         Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC         ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; L34345; AAA25324.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59545; -.
DR   SMR; Q59545; -.
DR   STRING; 582.AL531_10925; -.
DR   BioCyc; MetaCyc:MON-12199; -.
DR   GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05285; sorbitol_DH; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..338
FT                   /note="D-xylulose reductase"
FT                   /id="PRO_0000160885"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  35952 MW;  4C6119553DC51873 CRC64;
     MIMKALVLEK AGKIAIQDWQ SNEVLGDDDV EIKIHTVGIC GSDVHYYQHG RIGPFVVDEP
     MVLGHEASGV ITAAGKNVKH LKVGDRVCME PGIPDLQSPQ SRAGIYNLDP AVRFWATPPI
     DGCLRESVIH PAAFTFKLPD NVSFAQGAMV EPLAIGMQSA TKAGIKPGDI GLVIGAGTIG
     IITQSALAGG CSDVIICDVF DEKLKVAEKY QGLHAVNSKD QQALADKVRE LTGGEGVNVL
     FECSGAKPVI ASISDHIAPG GTAVLVGMPI DPAPLDIVAA QAKEVTFKTI LRYANMYPRT
     IRLLSSGKLN VAPLLSATYK FKDSVEAYER AAEPVRLM