ID   XYL1_PACTA              Reviewed;         318 AA.
AC   P78736;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=NAD(P)H-dependent D-xylose reductase;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=XYL1;
OS   Pachysolen tannophilus (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX   NCBI_TaxID=4918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 32691 / BCRC 20329 / CBS 4044 / DSM 70352 / NBRC 1007 / NRRL
RC   Y-2460;
RX   PubMed=8923742;
RX   DOI=10.1002/(sici)1097-0061(199610)12:13<1367::aid-yea33>3.0.co;2-#;
RA   Bolen P.L., Hayman G., Shepherd H.S.;
RT   "Sequence and analysis of an aldose (xylose) reductase gene from the
RT   xylose-fermenting yeast Pachysolen tannophilus.";
RL   Yeast 12:1367-1375(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-62.
RA   Bolen P.L., Bietz J.A., Detroy R.W.;
RT   "Aldose reductase in the yeast Pachysolen tannophilus: purification,
RT   characterization and N-terminal sequence.";
RL   Biotechnol. Bioeng. Symp. 15:129-148(1985).
CC   -!- FUNCTION: Reduces D-xylose into xylitol. Has a preference for NADPH,
CC       but can also utilize NADH as cosubstrate (By similarity).
CC       {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; U40706; AAC49526.1; -; mRNA.
DR   AlphaFoldDB; P78736; -.
DR   SMR; P78736; -.
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; 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.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; NAD; NADP;
KW   Oxidoreductase; Xylose metabolism.
FT   CHAIN           1..318
FT                   /note="NAD(P)H-dependent D-xylose reductase"
FT                   /id="PRO_0000124665"
FT   ACT_SITE        48
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            77
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  36422 MW;  891FC6F461D231EC CRC64;
     MTLQYYTLNN GRKIPAIGMG CWKLENAADM VYAAIKEGYR LFDCACDYGN EKEVGEGINR
     AIKDGLVKRK DLFITSKLWN NFHAKENVKK ALMKSLSDFN LDYFDLYLMH FPISFKFVPF
     EEKYPPGFYC GDGDKFIYED VPIIETWRAM ENLVDEGLVK SIGVSNVSGG LLEDLIKAAR
     IKPASLQIEH HPYLQQNKLV EYAQLKGIVV TGYSNFGPLS FLELGNETAK KTQPLYENKT
     ITTIAAKHGK TPFQVLLRWV NQRGIAIIPK STFPNTLAVN LHVDEFDLTK EDFEEIAKLD
     RHLRFNDPWT WDKIPTFV