XYL1_PICGU
ID XYL1_PICGU Reviewed; 317 AA.
AC O94735; A5DCB7; Q2V572;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=NADPH-dependent D-xylose reductase;
DE Short=XR;
DE EC=1.1.1.307;
GN Name=XYL1; ORFNames=PGUG_00922;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 20118 / CBS 6319 / IFO 0838 / JCM 2298 / NCYC 1399;
RX PubMed=9615481; DOI=10.1007/s002530051189;
RA Handumrongkul C., Ma D.-P., Silva J.L.;
RT "Cloning and expression of Candida guilliermondii xylose reductase gene
RT (xyl1) in Pichia pastoris.";
RL Appl. Microbiol. Biotechnol. 49:399-404(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Guo C., He P., Lu D., Shen A., Jiang N.;
RT "Isolation and phylogenetic relationship of aldose reductase in Candida
RT species.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Reduces D-xylose into xylitol. Preferentially utilizes NADPH
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}.
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; AF020040; AAD09330.1; -; mRNA.
DR EMBL; DQ297454; ABB87187.1; -; Genomic_DNA.
DR EMBL; CH408155; EDK36824.1; -; Genomic_DNA.
DR RefSeq; XP_001487545.1; XM_001487495.1.
DR AlphaFoldDB; O94735; -.
DR SMR; O94735; -.
DR STRING; 4929.XP_001487545.1; -.
DR EnsemblFungi; EDK36824; EDK36824; PGUG_00922.
DR GeneID; 5128729; -.
DR KEGG; pgu:PGUG_00922; -.
DR VEuPathDB; FungiDB:PGUG_00922; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; O94735; -.
DR OMA; AFKPGNE; -.
DR OrthoDB; 1016440at2759; -.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000001997; 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; 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; NADP; Oxidoreductase; Reference proteome;
KW Xylose metabolism.
FT CHAIN 1..317
FT /note="NADPH-dependent D-xylose reductase"
FT /id="PRO_0000124666"
FT ACT_SITE 47
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 213..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 269..279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 76
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="T -> K (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="E -> D (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="K -> N (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="K -> R (in Ref. 2; ABB87187)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="E -> D (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> P (in Ref. 2; ABB87187)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="R -> K (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="I -> H (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="I -> T (in Ref. 2; ABB87187)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="G -> D (in Ref. 1; AAD09330 and 2; ABB87187)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="I -> L (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="M -> L (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> S (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> S (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="I -> V (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="N -> D (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..248
FT /note="EKAN -> GKVK (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="K -> Q (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="V -> I (in Ref. 1; AAD09330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 36086 MW; DA18DF2A03186327 CRC64;
MSITLNSGYE MPSVGFGCWK VDKATCADTI YNAIKVGYRL FDGAEDYGNE KEVGEGINRA
LDEGLVARDE LFVVSKLWNS FHDPKNVEKA LDRTLSDLKV DYLDLFLIHF PIAFKFVPFE
EKYPPGFYCG DGDKFIYEGV PIIDTWRALE KMVEKGKIRS IGISNFPGAL IQDLLRGAKI
KPAVLQIEHH PYLQQPRLIE YVQSQGIAIT AYSSFGPQSF VELNHPRVKD VKPLFEHDVI
KSVAEKANKT PAQVLLRWAT QRGLAVIPKS NNPDRLLSNL KVNDFDLSQE DFKEISKLDI
ELRFNNPWDW DKIPTFV
