ID   XYL2_ASPNG              Reviewed;         358 AA.
AC   Q5GN51;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=D-xylulose reductase A;
DE            EC=1.1.1.9;
DE   AltName: Full=Xylitol dehydrogenase A;
GN   Name=xdhA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 513.88;
RA   de Groot M.J.L., Vandeputte-Rutten L., van den Dool C., Woesten H.A.B.,
RA   Levisson M., vanKuyk P.A., Ruijter G.J.G., de Vries R.P.;
RT   "Diversity in regulation and substrate specificity of the pentose catabolic
RT   pathway genes/enzymes of Aspergillus niger.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Xylitol dehydrogenase which catalyzes the conversion of
CC       xylitol to D-xylulose. Xylose is a major component of hemicelluloses
CC       such as xylan. Most fungi utilize D-xylose via three enzymatic
CC       reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and
CC       xylulokinase, to form xylulose 5-phosphate, which enters pentose
CC       phosphate pathway (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC       step 4/5.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ854041; CAH69384.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5GN51; -.
DR   SMR; Q5GN51; -.
DR   STRING; 5061.CADANGAP00009275; -.
DR   VEuPathDB; FungiDB:An12g00030; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1143012; -.
DR   VEuPathDB; FungiDB:ATCC64974_39060; -.
DR   VEuPathDB; FungiDB:M747DRAFT_293400; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   BioCyc; MetaCyc:MON-21872; -.
DR   UniPathway; UPA00146; UER00577.
DR   GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW   Xylose metabolism; Zinc.
FT   CHAIN           1..358
FT                   /note="D-xylulose reductase A"
FT                   /id="PRO_0000393510"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         182..187
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  37912 MW;  8EE8466F840C9399 CRC64;
     MSTQNTNAQN LSFVLEGIHR VKFEDRPIPE INNPHDVLVN VRFTGICGSD VHYWEHGSIG
     QFIVKDPMVL GHESSGVVSK VGSAVTSLKV GDCVAMEPGI PCRRCEPCKA GKYNLCVKMA
     FAATPPYDGT LAKYYVLPED FCYKLPESIT LQEGAIMEPL SVAVHIVKQA GINPGQSVVV
     FGAGPVGLLC CAVAKAYGAS KVIAVDIQKG RLDFAKKYAA TATFEPAKAA ALENAQRIIT
     ENDLGSGADV AIDASGAEPS VHTGIHVLRA GGTYVQGGMG RSEITFPIMA ACTKELNVKG
     SFRYGSGDYK LAVSLVSAGK VNVKELITGV VKFEDAERAF EEVRAGKGIK TLIAGVDS