XYL2_ASPNC
ID XYL2_ASPNC Reviewed; 358 AA.
AC A2QY54;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable D-xylulose reductase A;
DE EC=1.1.1.9;
DE AltName: Full=Xylitol dehydrogenase A;
GN Name=xdhA; ORFNames=An12g00030;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270258; CAK40934.1; -; Genomic_DNA.
DR RefSeq; XP_001395093.1; XM_001395056.2.
DR AlphaFoldDB; A2QY54; -.
DR SMR; A2QY54; -.
DR PaxDb; A2QY54; -.
DR EnsemblFungi; CAK40934; CAK40934; An12g00030.
DR GeneID; 4985352; -.
DR KEGG; ang:ANI_1_4104; -.
DR VEuPathDB; FungiDB:An12g00030; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR UniPathway; UPA00146; UER00577.
DR Proteomes; UP000006706; Chromosome 3L.
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 Reference proteome; Xylose metabolism; Zinc.
FT CHAIN 1..358
FT /note="Probable D-xylulose reductase A"
FT /id="PRO_0000393509"
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
