ID   XYL2_PIG                Reviewed;         134 AA.
AC   P83049;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   02-JUN-2021, entry version 46.
DE   RecName: Full=D-xylulose reductase;
DE            EC=1.1.1.9;
DE   AltName: Full=Xylitol dehydrogenase;
DE            Short=XDH;
DE   Flags: Fragments;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND ACTIVITY REGULATION.
RC   TISSUE=Kidney;
RA   Schweiger M., Wissler J.H., Amselgruber W.M.;
RT   "Xylitol:NAD 2-oxidoreductase (D-xylulose reductase EC 1.1.1.9) from
RT   porcine kidney. Purification and properties.";
RL   Submitted (JUL-2001) to UniProtKB.
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   -!- ACTIVITY REGULATION: Activated by calcium and inhibited by zinc.
CC       {ECO:0000269|Ref.1, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome; Xylose metabolism; Zinc.
FT   CHAIN           1..>134
FT                   /note="D-xylulose reductase"
FT                   /id="PRO_0000160882"
FT   REGION          29..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        55..56
FT                   /evidence="ECO:0000305"
FT   NON_CONS        68..69
FT                   /evidence="ECO:0000305"
FT   NON_CONS        76..77
FT                   /evidence="ECO:0000305"
FT   NON_CONS        80..81
FT                   /evidence="ECO:0000305"
FT   NON_CONS        92..93
FT                   /evidence="ECO:0000305"
FT   NON_CONS        110..111
FT                   /evidence="ECO:0000305"
FT   NON_CONS        128..129
FT                   /evidence="ECO:0000305"
FT   NON_TER         134
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   134 AA;  14858 MW;  540FC39ADDBFB5DA CRC64;
     XXKLVESGXX LVQPGGSLRL SKXYTENVNH PATTTXYKXQ PMTPDFTEXQ THEGTHQDVF
     DQPNLXXWKG NTLPEGYEPA KXGEXGTQDA NPKXXQDGDE XTXTGXXQXD KIGRYNLXPT
     IFFEATPPKA NENQ