XYL1_HYPJE
ID XYL1_HYPJE Reviewed; 324 AA.
AC Q876L8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=NAD(P)H-dependent D-xylose reductase xyl1;
DE Short=XR;
DE EC=1.1.1.-;
GN Name=xyl1;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX PubMed=17924946; DOI=10.1111/j.1365-2958.2007.05953.x;
RA Seiboth B., Gamauf C., Pail M., Hartl L., Kubicek C.P.;
RT "The D-xylose reductase of Hypocrea jecorina is the major aldose reductase
RT in pentose and D-galactose catabolism and necessary for beta-galactosidase
RT and cellulase induction by lactose.";
RL Mol. Microbiol. 66:890-900(2007).
CC -!- FUNCTION: Catalyzes the initial reaction in the xylose utilization
CC pathway by reducing D-xylose into xylitol. Xylose is a major component
CC of hemicelluloses such as xylan. Most fungi utilize D-xylose via three
CC enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase
CC (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters
CC pentose phosphate pathway. Also major aldose reductase in pentose and
CC D-galactose catabolism. Reduces the pentose L-arabinose and the hexose
CC D-galactose to their respective polyols. Responsible for extracellular
CC beta-galactosidase formation and cellulase induction during growth on
CC lactose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + NAD(+) = an aldose + H(+) + NADH;
CC Xref=Rhea:RHEA:12785, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:17924946};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH;
CC Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:17924946};
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 Evidence={ECO:0000269|PubMed:17924946};
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 Evidence={ECO:0000269|PubMed:17924946};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 mM for D-xylose {ECO:0000269|PubMed:17924946};
CC KM=24 mM for D-ribose {ECO:0000269|PubMed:17924946};
CC KM=41 mM for L-arabinose {ECO:0000269|PubMed:17924946};
CC KM=82 mM for D-galactose {ECO:0000269|PubMed:17924946};
CC KM=366 mM for D-glucose {ECO:0000269|PubMed:17924946};
CC KM=11 mM for xylitol {ECO:0000269|PubMed:17924946};
CC KM=76 mM for L-arabinitol {ECO:0000269|PubMed:17924946};
CC KM=155 mM for galactitol {ECO:0000269|PubMed:17924946};
CC KM=98 mM for ribitol {ECO:0000269|PubMed:17924946};
CC KM=159 mM for D-sorbitol {ECO:0000269|PubMed:17924946};
CC KM=0.023 mM for NADPH {ECO:0000269|PubMed:17924946};
CC KM=0.26 mM for NADH {ECO:0000269|PubMed:17924946};
CC Vmax=176 nmol/sec/mg enzyme toward NADPH
CC {ECO:0000269|PubMed:17924946};
CC Vmax=0.42 nmol/sec/mg enzyme toward NADH
CC {ECO:0000269|PubMed:17924946};
CC Vmax=225 nmol/sec/mg enzyme with D-xylose as substrate for the
CC reverse reaction {ECO:0000269|PubMed:17924946};
CC Vmax=9 nmol/sec/mg enzyme with xylitol as substrate for the forward
CC reaction {ECO:0000269|PubMed:17924946};
CC Vmax=125 nmol/sec/mg enzyme with ribose as substrate for the reverse
CC reaction {ECO:0000269|PubMed:17924946};
CC Vmax=9 nmol/sec/mg enzyme with ribitol as substrate for the forward
CC reaction {ECO:0000269|PubMed:17924946};
CC Vmax=175 nmol/sec/mg enzyme with L-arabinose as substrate for the
CC reverse reaction {ECO:0000269|PubMed:17924946};
CC Vmax=16 nmol/sec/mg enzyme with L-arabinitol as substrate for the
CC forward reaction {ECO:0000269|PubMed:17924946};
CC Vmax=18 nmol/sec/mg enzyme with D-galactose as substrate for the
CC reverse reaction {ECO:0000269|PubMed:17924946};
CC Vmax=9 nmol/sec/mg enzyme with galactitol as substrate for the
CC forward reaction {ECO:0000269|PubMed:17924946};
CC Vmax=66 nmol/sec/mg enzyme with D-glucose as substrate for the
CC reverse reaction {ECO:0000269|PubMed:17924946};
CC Vmax=18 nmol/sec/mg enzyme with D-sorbitol as substrate for the
CC forward reaction {ECO:0000269|PubMed:17924946};
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC step 1/5.
CC -!- INDUCTION: Regulated by carbon source. Most abundant during growth on
CC D-xylose and L-arabinose. {ECO:0000269|PubMed:17924946}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AY116507; AAM66765.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876L8; -.
DR SMR; Q876L8; -.
DR OMA; ECGEGVA; -.
DR BioCyc; MetaCyc:MON-16170; -.
DR BRENDA; 1.1.1.307; 6451.
DR SABIO-RK; Q876L8; -.
DR UniPathway; UPA00146; UER00574.
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 GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR CDD; cd19115; AKR_AKR2D1; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044487; AKR2D.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Xylose metabolism.
FT CHAIN 1..324
FT /note="NAD(P)H-dependent D-xylose reductase xyl1"
FT /id="PRO_0000124668"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 217..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 273..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 36565 MW; FC615DAA7B90E26E CRC64;
MASPTLKLNS GYDMPQVGFG LWKVDNAVCA DTVYNAIKAG YRLFDGACDY GNEKECGEGV
ARAIKDGLVK REDLFIVSKL WQTFHDEDKV EPITRRQLAD WQIDYFDLFL VHFPAALEYV
DPSVRYPPGW FYDGKSEVRW SKTTTLQQTW GAMERLVDKG LARSIGVSNY QAQSVYDALI
YARIKPATLQ IEHHPYLQQP DLVSLAQTEG IVVTAYSSFG PTGFMELDMP RAKSVAPLMD
SPVIKALADK HRRTPAQVLL RWATQRGIAV IPKTSRPEVM AQNLDNTSFD LDSEDLAKIA
DMDLNIRFNK PTNYFSANKL YLFG
