XYL1_PICST
ID XYL1_PICST Reviewed; 318 AA.
AC P31867; A3LVN7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=NAD(P)H-dependent D-xylose reductase;
DE Short=XR;
DE EC=1.1.1.307;
GN Name=XYL1; ORFNames=PICST_89614;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542;
RX PubMed=1756986; DOI=10.1016/0378-1119(91)90592-y;
RA Amore R., Koetter P., Kuester C., Ciriacy M., Hollenberg C.P.;
RT "Cloning and expression in Saccharomyces cerevisiae of the NAD(P)H-
RT dependent xylose reductase-encoding gene (XYL1) from the xylose-
RT assimilating yeast Pichia stipitis.";
RL Gene 109:89-97(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3921014; DOI=10.1042/bj2260669;
RA Verduyn C., Van Kleef R., Frank J., Schreuder H., Van Dijken J.P.,
RA Scheffers W.A.;
RT "Properties of the NAD(P)H-dependent xylose reductase from the xylose-
RT fermenting yeast Pichia stipitis.";
RL Biochem. J. 226:669-677(1985).
CC -!- FUNCTION: Reduces D-xylose into xylitol. Has a preference for NADPH,
CC but can also utilize NADH as cosubstrate. {ECO:0000269|PubMed:3921014}.
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 -!- ACTIVITY REGULATION: NADP(+) is a potent inhibitor of both the
CC NADPH- and NADH-linked xylose reduction, whereas NAD(+) showS strong
CC inhibition only with the NADH-linked reaction.
CC {ECO:0000269|PubMed:3921014}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 mM for D-Xylose {ECO:0000269|PubMed:3921014};
CC KM=9 uM for NADPH {ECO:0000269|PubMed:3921014};
CC KM=21 mM for NADH {ECO:0000269|PubMed:3921014};
CC KM=18 mM for DL-Glyceraldehyde {ECO:0000269|PubMed:3921014};
CC KM=40 mM for L-Arabinose {ECO:0000269|PubMed:3921014};
CC KM=310 mM for D-Ribose {ECO:0000269|PubMed:3921014};
CC KM=140 mM for D-Galactose {ECO:0000269|PubMed:3921014};
CC KM=420 mM for D-Glucose {ECO:0000269|PubMed:3921014};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:3921014};
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; X59465; CAA42072.1; -; Genomic_DNA.
DR EMBL; CP000499; ABN67152.1; -; Genomic_DNA.
DR PIR; JQ1387; JQ1387.
DR RefSeq; XP_001385181.1; XM_001385144.1.
DR PDB; 5Z6T; X-ray; 2.00 A; A/B=1-318.
DR PDB; 5Z6U; X-ray; 1.95 A; A/B=1-318.
DR PDBsum; 5Z6T; -.
DR PDBsum; 5Z6U; -.
DR AlphaFoldDB; P31867; -.
DR SMR; P31867; -.
DR STRING; 4924.XP_001385181.1; -.
DR PRIDE; P31867; -.
DR EnsemblFungi; ABN67152; ABN67152; PICST_89614.
DR GeneID; 4839234; -.
DR KEGG; pic:PICST_89614; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P31867; -.
DR OMA; ECGEGVA; -.
DR OrthoDB; 1016440at2759; -.
DR BioCyc; MetaCyc:MON-15496; -.
DR BRENDA; 1.1.1.307; 4832.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000002258; Chromosome 5.
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 3D-structure; Carbohydrate metabolism; NAD; NADP; Oxidoreductase;
KW Reference proteome; Xylose metabolism.
FT CHAIN 1..318
FT /note="NAD(P)H-dependent D-xylose reductase"
FT /id="PRO_0000124667"
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"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:5Z6U"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5Z6U"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5Z6U"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:5Z6U"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:5Z6U"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:5Z6T"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:5Z6U"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:5Z6U"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:5Z6U"
SQ SEQUENCE 318 AA; 35923 MW; 0059EF145C655976 CRC64;
MPSIKLNSGY DMPAVGFGCW KVDVDTCSEQ IYRAIKTGYR LFDGAEDYAN EKLVGAGVKK
AIDEGIVKRE DLFLTSKLWN NYHHPDNVEK ALNRTLSDLQ VDYVDLFLIH FPVTFKFVPL
EEKYPPGFYC GKGDNFDYED VPILETWKAL EKLVKAGKIR SIGVSNFPGA LLLDLLRGAT
IKPSVLQVEH HPYLQQPRLI EFAQSRGIAV TAYSSFGPQS FVELNQGRAL NTSPLFENET
IKAIAAKHGK SPAQVLLRWS SQRGIAIIPK SNTVPRLLEN KDVNSFDLDE QDFADIAKLD
INLRFNDPWD WDKIPIFV
