ID   XYL1_ASPFN              Reviewed;         319 AA.
AC   B8N195;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Probable NAD(P)H-dependent D-xylose reductase xyl1;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=xyl1; ORFNames=AFLA_029600;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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   -!- 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   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ963473; EED55688.1; -; Genomic_DNA.
DR   RefSeq; XP_002374470.1; XM_002374429.1.
DR   AlphaFoldDB; B8N195; -.
DR   SMR; B8N195; -.
DR   STRING; 5059.CADAFLAP00002335; -.
DR   EnsemblFungi; EED55688; EED55688; AFLA_029600.
DR   VEuPathDB; FungiDB:AFLA_029600; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   OMA; AFKPGNE; -.
DR   UniPathway; UPA00810; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Xylose metabolism.
FT   CHAIN           1..319
FT                   /note="Probable NAD(P)H-dependent D-xylose reductase xyl1"
FT                   /id="PRO_0000393498"
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;  35868 MW;  348BB434877572C2 CRC64;
     MASPTVKLNS GHDMPLVGFG LWKVNNETCA DQVYEAIKAG YRLFDGACDY GNEVECGQGV
     ARAIKEGIVK REELFIVSKL WNSFHEGDRV EPICRKQLAD WGVDYFDLYI VHFPVALKYV
     DPAVRYPPGW NSESGKIEFS NATIQETWTA MESLVDKKLA RSIGVSNFSA QLLMDLLRYA
     RVRPATLQIE HHPYLTQPRL VEYAQKEGIA VTAYSSFGPL SFLELEVKNA VDTPPLFEHN
     TIKSLAEKYG KTPAQVLLRW ATQRGIAVIP KSNNPTRLSQ NLEVTGWDLE KSELEAISSL
     DKGLRFNDPI GYGMYVPIF