ID   XYL1_CANPA              Reviewed;         324 AA.
AC   Q6Y0Z3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=NADH-dependent D-xylose reductase;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=XYL1;
OS   Candida parapsilosis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=KFCC-10875;
RX   PubMed=14532079; DOI=10.1128/aem.69.10.6179-6188.2003;
RA   Lee J.K., Koo B.S., Kim S.Y.;
RT   "Cloning and characterization of the xyl1 gene, encoding an NADH-preferring
RT   xylose reductase from Candida parapsilosis, and its functional expression
RT   in Candida tropicalis.";
RL   Appl. Environ. Microbiol. 69:6179-6188(2003).
CC   -!- FUNCTION: Reduces D-xylose into xylitol. Preferentially utilizes NADH
CC       as a cosubstrate.
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; AY193716; AAO91803.1; -; mRNA.
DR   AlphaFoldDB; Q6Y0Z3; -.
DR   SMR; Q6Y0Z3; -.
DR   KEGG; ag:AAO91803; -.
DR   VEuPathDB; FungiDB:CPAR2_101350; -.
DR   BioCyc; MetaCyc:MON-21874; -.
DR   BRENDA; 1.1.1.307; 1133.
DR   UniPathway; UPA00810; -.
DR   GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:EnsemblFungi.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0019568; P:arabinose catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019388; P:galactose catabolic process; IEA:EnsemblFungi.
DR   CDD; cd19113; AKR_AKR2B1-10; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044486; AKR2B1.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; NAD; Oxidoreductase;
KW   Xylose metabolism.
FT   CHAIN           1..324
FT                   /note="NADH-dependent D-xylose reductase"
FT                   /id="PRO_0000124659"
FT   ACT_SITE        54
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            83
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36629 MW;  C64951D131707E19 CRC64;
     MSTATASPAV KLNSGYEIPL VGFGCWKLTN DVASDQIYRA IKSGYRLFDG AEDYANEQEV
     GEGIKRAIKE GIVKREELFI TSKLWNSFHD KKNVEVALMK TLSDLNLDYV DLFYIHFPIA
     QKPVPIEKKY PPGFYCGDGD KWSIEEVPLL DTWRALEKLV DQGLAKSIGI SNFSAQLIYD
     LIRGCTIKPV ALQIEHHPYL TQPKLVEYVQ LHDIQITGYS SFGPQSFLEM DLKRALDTPV
     LLEEPTVKSI ADKHGKSPAQ VLLRYQTQRG IAVIPRSNSP DRMAQNLSVI DFELTQDDLQ
     AIAELDCNLR FNEPWDFSNI PVFV