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XYL1_CANBO
ID   XYL1_CANBO              Reviewed;         321 AA.
AC   Q8X195;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=NADPH-dependent D-xylose reductase;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=XYL1; Synonyms=cbXR;
OS   Candida boidinii (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX   NCBI_TaxID=5477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=NRRL Y-17213;
RX   PubMed=12721450; DOI=10.1385/abab:106:1-3:265;
RA   Kang M.H., Ni H., Jeffries T.W.;
RT   "Molecular characterization of a gene for aldose reductase (CbXYL1) from
RT   Candida boidinii and its expression in Saccharomyces cerevisiae.";
RL   Appl. Biochem. Biotechnol. 106:265-276(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=NRRL Y-17213;
RX   PubMed=16838379; DOI=10.1002/bit.21082;
RA   Cirino P.C., Chin J.W., Ingram L.O.;
RT   "Engineering Escherichia coli for xylitol production from glucose-xylose
RT   mixtures.";
RL   Biotechnol. Bioeng. 95:1167-1176(2006).
RN   [3]
RP   FUNCTION.
RX   PubMed=18359531; DOI=10.1016/j.jbiotec.2008.02.003;
RA   Khankal R., Chin J.W., Cirino P.C.;
RT   "Role of xylose transporters in xylitol production from engineered
RT   Escherichia coli.";
RL   J. Biotechnol. 134:246-252(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=18698648; DOI=10.1002/bit.22060;
RA   Chin J.W., Khankal R., Monroe C.A., Maranas C.D., Cirino P.C.;
RT   "Analysis of NADPH supply during xylitol production by engineered
RT   Escherichia coli.";
RL   Biotechnol. Bioeng. 102:209-220(2009).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, DOMAIN, AND
RP   MUTAGENESIS OF 272-LYS--ASN-274.
RX   PubMed=19693930; DOI=10.1002/pro.227;
RA   Khoury G.A., Fazelinia H., Chin J.W., Pantazes R.J., Cirino P.C.,
RA   Maranas C.D.;
RT   "Computational design of Candida boidinii xylose reductase for altered
RT   cofactor specificity.";
RL   Protein Sci. 18:2125-2138(2009).
CC   -!- FUNCTION: Reduces D-xylose into xylitol. Preferentially utilizes NADPH
CC       as a cosubstrate. {ECO:0000269|PubMed:12721450,
CC       ECO:0000269|PubMed:16838379, ECO:0000269|PubMed:18359531,
CC       ECO:0000269|PubMed:18698648, ECO:0000269|PubMed:19693930}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=307 uM for NADPH {ECO:0000269|PubMed:19693930};
CC         Vmax=152 nmol/min/mg enzyme (in the presence of NADPH)
CC         {ECO:0000269|PubMed:19693930};
CC         Note=Mutations at positions 272 to 274 modify the cofactor
CC         specificity and increase specificity for NADH over NADPH.;
CC   -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC   -!- DOMAIN: The Lys-Ser-Asn motif at positions 272 to 274 is important for
CC       the cofactor specificity for NADPH over NADH.
CC       {ECO:0000269|PubMed:19693930}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AF451326; AAL47846.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X195; -.
DR   SMR; Q8X195; -.
DR   OrthoDB; 1016440at2759; -.
DR   BRENDA; 1.1.1.307; 1100.
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.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Xylose metabolism.
FT   CHAIN           1..321
FT                   /note="NADPH-dependent D-xylose reductase"
FT                   /id="PRO_0000407987"
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="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..225
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         272..282
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         272..274
FT                   /note="KSN->EDR: Increases cofactor specificity for NADH
FT                   over NADPH 240 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->EDR: Increases cofactor specificity for NADH
FT                   over NADPH more than 1900 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->EDS: Increases cofactor specificity for NADH
FT                   over NADPH 240 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->EQR: Increases cofactor specificity for NADH
FT                   over NADPH 6 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->GGD: Increases cofactor specificity for NADH
FT                   over NADPH 440 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->MAE: Increases cofactor specificity for NADH
FT                   over NADPH more than 5400 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->MES: Increases cofactor specificity for NADH
FT                   over NADPH more than 1800 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->MGD: Increases cofactor specificity for NADH
FT                   over NADPH 890 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->REG: Increases cofactor specificity for NADH
FT                   over NADPH more than 11200 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->RSE: Increases cofactor specificity for NADH
FT                   over NADPH 37 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272..274
FT                   /note="KSN->RTT: Increases cofactor specificity for NADH
FT                   over NADPH 13 times."
FT                   /evidence="ECO:0000269|PubMed:19693930"
FT   MUTAGEN         272
FT                   /note="K->R: Increases cofactor specificity for NADH over
FT                   NADPH 50 times."
SQ   SEQUENCE   321 AA;  36470 MW;  FCFA8F2A900C86EB CRC64;
     MSSPLLTLNN GLKMPQIGFG CWKVDNATCA ETIYEAIKVG YRLFDGAMDY GNEKEVGEGV
     NKAIKDGLVK REELFIVSKL WNNFHHPDSV KLAIKKVLSD LNLEYIDLFY MHFPIAQKFV
     PIEKKYPPNF YCGDGDKWSF EDVPLLTTWR AMEELVEEGL VKSIGISNFV GALIQDLLRG
     CKIRPAVLEI EHHPYLVQPR LIEYAKTEGI HVTAYSSFGP QSFVELDHPK VKDCTTLFKH
     ETITSIASAH DVPPAKVLLR WATQRGLAVI PKSNKKERLL GNLKINDFDL TEAELEKIEA
     LDIGLRFNDP WTWGYNIPTF I
 
 
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