ID   XYL1_ASPNG              Reviewed;         319 AA.
AC   Q9P8R5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=NAD(P)H-dependent D-xylose reductase xyl1;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=xyl1; Synonyms=xyrA;
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], FUNCTION, AND INDUCTION.
RX   PubMed=10760176; DOI=10.1046/j.1365-2958.2000.01843.x;
RA   Hasper A.A., Visser J., de Graaff L.H.;
RT   "The Aspergillus niger transcriptional activator XlnR, which is involved in
RT   the degradation of the polysaccharides xylan and cellulose, also regulates
RT   D-xylose reductase gene expression.";
RL   Mol. Microbiol. 36:193-200(2000).
CC   -!- FUNCTION: Catalyzes the initial reaction in the xylose utilization
CC       pathway by reducing D-xylose into xylitol. Xylose is a major component
CC       of hemicelluloses such as xylan. Most fungi utilize D-xylose via three
CC       enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase
CC       (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters
CC       pentose phosphate pathway (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:10760176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH;
CC         Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.307;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH;
CC         Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.307;
CC   -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC   -!- INDUCTION: Expression controlled by the xylanolytic transcriptional
CC       activator xlnR. {ECO:0000269|PubMed:10760176}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AF219625; AAF61912.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P8R5; -.
DR   SMR; Q9P8R5; -.
DR   STRING; 5061.CADANGAP00000355; -.
DR   VEuPathDB; FungiDB:An01g03740; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1156486; -.
DR   VEuPathDB; FungiDB:ATCC64974_20080; -.
DR   VEuPathDB; FungiDB:M747DRAFT_265636; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   BRENDA; 1.1.1.307; 518.
DR   UniPathway; UPA00810; -.
DR   GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:InterPro.
DR   GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd19115; AKR_AKR2D1; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044487; AKR2D.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; NAD; Oxidoreductase; Xylose metabolism.
FT   CHAIN           1..319
FT                   /note="NAD(P)H-dependent D-xylose reductase xyl1"
FT                   /id="PRO_0000124658"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..167
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  36095 MW;  C7D6DB56D37E973F CRC64;
     MASPTVKLNS GYDMPLVGFG LWKVNNDTCA DQIYHAIKEG YRLFDGACDY GNEVEAGQGI
     ARAIKDGLVK REELFIVSKL WNSFHDGDRV EPICRKQLAD WGIDYFDLYI VHFPISLKYV
     DPAVRYPPGW KSEKDELEFG NATIQETWTA MESLVDKKLA RSIGISNFSA QLVMDLLRYA
     RIRPATLQIE HHPYLTQTRL VEYAQKEGLT VTAYSSFGPL SFLELSVQNA VDSPPLFEHQ
     LVKSIAEKHG RTPAQVLLRW ATQRGIAVIP KSNNPQRLKQ NLDVTGWNLE EEEIKAISGL
     DRGLRFNDPL GYGLYAPIF