GRE3_YEAST
ID GRE3_YEAST Reviewed; 327 AA.
AC P38715; D3DL54;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=NADPH-dependent aldose reductase GRE3 {ECO:0000305|PubMed:11525399};
DE Short=AR {ECO:0000303|PubMed:11722921};
DE EC=1.1.1.21 {ECO:0000269|PubMed:7747971};
DE AltName: Full=Genes de respuesta a estres protein 3 {ECO:0000305|PubMed:10407268};
DE AltName: Full=NADPH-dependent aldo-keto reductase GRE3 {ECO:0000305|PubMed:7747971};
DE AltName: Full=Xylose reductase {ECO:0000303|PubMed:9730277};
DE EC=1.1.1.-;
GN Name=GRE3 {ECO:0000303|PubMed:10407268};
GN OrderedLocusNames=YHR104W {ECO:0000312|SGD:S000001146};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 2-14, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 26602;
RX PubMed=7747971; DOI=10.1128/aem.61.4.1580-1585.1995;
RA Kuhn A., van Zyl C., van Tonder A., Prior B.A.;
RT "Purification and partial characterization of an aldo-keto reductase from
RT Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 61:1580-1585(1995).
RN [4]
RP INDUCTION.
RX PubMed=10407268;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<879::aid-yea428>3.0.co;2-q;
RA Garay-Arroyo A., Covarrubias A.A.;
RT "Three genes whose expression is induced by stress in Saccharomyces
RT cerevisiae.";
RL Yeast 15:879-892(1999).
RN [5]
RP CATALYTIC ACTIVITY, ACTIVITY ON METHYLGLYOXAL, AND INDUCTION.
RX PubMed=11525399; DOI=10.1007/s002940100213;
RA Aguilera J., Prieto J.A.;
RT "The Saccharomyces cerevisiae aldose reductase is implied in the metabolism
RT of methylglyoxal in response to stress conditions.";
RL Curr. Genet. 39:273-283(2001).
RN [6]
RP ACTIVITY ON XYLOSE.
RX PubMed=11722921; DOI=10.1128/aem.67.12.5668-5674.2001;
RA Traff K.L., Otero Cordero R.R., van Zyl W.H., Hahn-Hagerdal B.;
RT "Deletion of the GRE3 aldose reductase gene and its influence on xylose
RT metabolism in recombinant strains of Saccharomyces cerevisiae expressing
RT the xylA and XKS1 genes.";
RL Appl. Environ. Microbiol. 67:5668-5674(2001).
RN [7]
RP REVIEW, AND XYLOSE UTILIZATION.
RX PubMed=9730277;
RX DOI=10.1002/(sici)1097-0061(199808)14:11<977::aid-yea302>3.0.co;2-j;
RA Lee H.;
RT "The structure and function of yeast xylose (aldose) reductases.";
RL Yeast 14:977-984(1998).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Aldose reductase with a broad substrate specificity. Reduces
CC the cytotoxic compound methylglyoxal (MG) to acetol and (R)-
CC lactaldehyde under stress conditions. MG is synthesized via a bypath of
CC glycolysis from dihydroxyacetone phosphate and is believed to play a
CC role in cell cycle regulation and stress adaptation (PubMed:11525399).
CC In pentose-fermenting yeasts, aldose reductase catalyzes the reduction
CC of xylose into xylitol. The purified enzyme catalyzes this reaction,
CC but the inability of S.cerevisiae to grow on xylose as sole carbon
CC source indicates that the physiological function is more likely
CC methylglyoxal reduction (Probable) (PubMed:11722921).
CC {ECO:0000269|PubMed:11525399, ECO:0000269|PubMed:11722921,
CC ECO:0000269|PubMed:7747971, ECO:0000305|PubMed:9730277}.
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; EC=1.1.1.21;
CC Evidence={ECO:0000269|PubMed:10407268, ECO:0000269|PubMed:7747971};
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; EC=1.1.1.21;
CC Evidence={ECO:0000269|PubMed:10407268, ECO:0000269|PubMed:7747971};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.046 mM for p-nitrobenzaldehyde {ECO:0000269|PubMed:7747971};
CC KM=1.44 mM for D-L-glyceraldehyde {ECO:0000269|PubMed:7747971};
CC KM=1.57 mM for D-glyceraldehyde {ECO:0000269|PubMed:7747971};
CC KM=6.38 mM for L-glyceraldehyde {ECO:0000269|PubMed:7747971};
CC KM=27.9 mM for D-xylose {ECO:0000269|PubMed:7747971};
CC KM=32.63 mM for L-arabinose {ECO:0000269|PubMed:7747971};
CC KM=9.34 mM for D-glucose {ECO:0000269|PubMed:7747971};
CC KM=0.013 mM for NADPH {ECO:0000269|PubMed:7747971};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:7747971};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7747971}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By osmotic, ionic, oxidative and heat stress.
CC {ECO:0000269|PubMed:10407268, ECO:0000269|PubMed:11525399}.
CC -!- MISCELLANEOUS: Present with 12851 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: 'De respuesta a estres' means stress response in
CC Spanish. {ECO:0000305|PubMed:10407268}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; U00059; AAB68858.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06798.1; -; Genomic_DNA.
DR PIR; S48946; S48946.
DR RefSeq; NP_011972.1; NM_001179234.1.
DR AlphaFoldDB; P38715; -.
DR SMR; P38715; -.
DR BioGRID; 36537; 158.
DR IntAct; P38715; 2.
DR MINT; P38715; -.
DR STRING; 4932.YHR104W; -.
DR iPTMnet; P38715; -.
DR MaxQB; P38715; -.
DR PaxDb; P38715; -.
DR PRIDE; P38715; -.
DR EnsemblFungi; YHR104W_mRNA; YHR104W; YHR104W.
DR GeneID; 856504; -.
DR KEGG; sce:YHR104W; -.
DR SGD; S000001146; GRE3.
DR VEuPathDB; FungiDB:YHR104W; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P38715; -.
DR OMA; AFKPGNE; -.
DR BioCyc; YEAST:YHR104W-MON; -.
DR BRENDA; 1.1.1.283; 984.
DR BRENDA; 1.1.1.307; 984.
DR PRO; PR:P38715; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38715; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:SGD.
DR GO; GO:0032866; F:D-xylose:NADP reductase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0019568; P:arabinose catabolic process; IDA:SGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0042843; P:D-xylose catabolic process; IDA:SGD.
DR GO; GO:0019388; P:galactose catabolic process; IGI:SGD.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
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 Cytoplasm; Direct protein sequencing; NADP; Nucleus; Oxidoreductase;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7747971"
FT CHAIN 2..327
FT /note="NADPH-dependent aldose reductase GRE3"
FT /id="PRO_0000124678"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 37119 MW; AFE72B8E2DFB91C8 CRC64;
MSSLVTLNNG LKMPLVGLGC WKIDKKVCAN QIYEAIKLGY RLFDGACDYG NEKEVGEGIR
KAISEGLVSR KDIFVVSKLW NNFHHPDHVK LALKKTLSDM GLDYLDLYYI HFPIAFKYVP
FEEKYPPGFY TGADDEKKGH ITEAHVPIID TYRALEECVD EGLIKSIGVS NFQGSLIQDL
LRGCRIKPVA LQIEHHPYLT QEHLVEFCKL HDIQVVAYSS FGPQSFIEMD LQLAKTTPTL
FENDVIKKVS QNHPGSTTSQ VLLRWATQRG IAVIPKSSKK ERLLGNLEIE KKFTLTEQEL
KDISALNANI RFNDPWTWLD GKFPTFA
