ID   XYL1_NEOFI              Reviewed;         321 AA.
AC   A1D4E3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=NFIA_019940;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW23286.1; -; Genomic_DNA.
DR   RefSeq; XP_001265183.1; XM_001265182.1.
DR   AlphaFoldDB; A1D4E3; -.
DR   SMR; A1D4E3; -.
DR   STRING; 36630.CADNFIAP00001734; -.
DR   EnsemblFungi; EAW23286; EAW23286; NFIA_019940.
DR   GeneID; 4591084; -.
DR   KEGG; nfi:NFIA_019940; -.
DR   VEuPathDB; FungiDB:NFIA_019940; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   OMA; AFKPGNE; -.
DR   OrthoDB; 1016440at2759; -.
DR   UniPathway; UPA00810; -.
DR   Proteomes; UP000006702; 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..321
FT                   /note="Probable NAD(P)H-dependent D-xylose reductase xyl1"
FT                   /id="PRO_0000393505"
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   321 AA;  36247 MW;  965BE509E3CBA6F0 CRC64;
     MTTPSTKLNS GYDMPLVGFG LWKVNNETCA DQIYHAIKAG YRLFDGACDY GNEVEAGKGV
     ARAIQEGIVK REDLFIVSKL WNSFHDGDRV EPICRKQLAD WGLDYFDLFI VHFPIALKYV
     DPAVRYPPGW LSENNKLEFS NASIQETWTA MESLVDKKLA RSIGVSNFSA QLLMDLLRYA
     RIRPATLQIE HHPYLTQERL VTYAQKEGIA VTAYSSFGPL SFVELDLKDA HETPKLFDHD
     VIKGIAQKHG KTPAQVLLRW ATQRNIAVIP KSNDPTRLAQ NLDVTGWDLE TSEIEVISSL
     NRNLRFNDPL APSRLDPIPD D