ID   XYL1_ASPTN              Reviewed;         320 AA.
AC   Q0CUL0;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ATEG_02624;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH476596; EAU37586.1; -; Genomic_DNA.
DR   RefSeq; XP_001211802.1; XM_001211802.1.
DR   AlphaFoldDB; Q0CUL0; -.
DR   SMR; Q0CUL0; -.
DR   STRING; 341663.Q0CUL0; -.
DR   EnsemblFungi; EAU37586; EAU37586; ATEG_02624.
DR   GeneID; 4317317; -.
DR   VEuPathDB; FungiDB:ATEG_02624; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   OMA; AFKPGNE; -.
DR   OrthoDB; 1016440at2759; -.
DR   UniPathway; UPA00810; -.
DR   Proteomes; UP000007963; 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; Reference proteome;
KW   Xylose metabolism.
FT   CHAIN           1..320
FT                   /note="Probable NAD(P)H-dependent D-xylose reductase xyl1"
FT                   /id="PRO_0000393502"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         272..282
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   320 AA;  35691 MW;  4BEC8BF29582E76D CRC64;
     MATPTIKLNS GFDMPLVGFG LWKVNNDTCA DQVYEAIKAG YRLFDGACDY GNEVEAGQGV
     ARAIKEGIVK REELFIVSKL WNSFHDGDKV EPICRKQLAD WGVDYFDLYI VHFPVALKYV
     DPAVRYPPGW SAKGDGSIEF SNASIQETWT AMETLVDKKL ARSIGVSNFS AQLLMDLLRY
     ARVRPATLQI EHHPYLTQPR LVEYAQKEGI AVTAYSSFGP LSFLELQVPN ATNISPLFEH
     DVVKSVADKH GKTPAQVLLR WSTQRGIAVI PKSNNPTRLS QNLEVTGWDL EQSEIDAISA
     LDIGLRFNDP IGYGMYVPIF