XYL1_KLULA
ID XYL1_KLULA Reviewed; 329 AA.
AC P49378;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NAD(P)H-dependent D-xylose reductase;
DE Short=XR;
DE EC=1.1.1.307;
GN Name=XYL1; OrderedLocusNames=KLLA0E21714g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=7557424; DOI=10.1016/0378-1119(95)00294-g;
RA Billard P., Menart S., Fleer R., Bolotin-Fukuhara M.;
RT "Isolation and characterization of the gene encoding xylose reductase from
RT Kluyveromyces lactis.";
RL Gene 162:93-97(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Reduces D-xylose into xylitol.
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; L36993; AAA99507.1; -; Genomic_DNA.
DR EMBL; CR382125; CAH00016.1; -; Genomic_DNA.
DR PIR; JC4251; JC4251.
DR RefSeq; XP_454929.1; XM_454929.1.
DR AlphaFoldDB; P49378; -.
DR SMR; P49378; -.
DR STRING; 28985.XP_454929.1; -.
DR EnsemblFungi; CAH00016; CAH00016; KLLA0_E21627g.
DR GeneID; 2894271; -.
DR KEGG; kla:KLLA0_E21627g; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P49378; -.
DR OMA; AFKPGNE; -.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000000598; Chromosome E.
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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome;
KW Xylose metabolism.
FT CHAIN 1..329
FT /note="NAD(P)H-dependent D-xylose reductase"
FT /id="PRO_0000124664"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 222..231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 278..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 81
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 37516 MW; A63C166D7B478D43 CRC64;
MTYLAETVTL NNGEKMPLVG LGCWKMPNDV CADQIYEAIK IGYRLFDGAQ DYANEKEVGQ
GVNRAIKEGL VKREDLVVVS KLWNSFHHPD NVPRALERTL SDLQLDYVDI FYIHFPLAFK
PVPFDEKYPP GFYTGKEDEA KGHIEEEQVP LLDTWRALEK LVDQGKIKSL GISNFSGALI
QDLLRGARIK PVALQIEHHP YLTQERLIKY VKNAGIQVVA YSSFGPVSFL ELENKKALNT
PTLFEHDTIK SIASKHKVTP QQVLLRWATQ NGIAIIPKSS KKERLLDNLR INDALTLTDD
ELKQISGLNQ NIRFNDPWEW LDNEFPTFI
