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UniProtKB/Swiss-Prot entry P38715

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRE3_YEAST
Primary accession number P38715
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 73)
Name and origin of the protein
Protein name NADPH-dependent aldose reductase GRE3
Synonyms EC 1.1.1.21
NADPH-dependent aldo-keto reductase GRE3
NADPH-dependent methylglyoxal reductase GRE3
Xylose reductase
EC 1.1.1.-
Genes de respuesta a estres protein 3
Gene name
Name: GRE3
OrderedLocusNames: YHR104W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[2]
 INDUCTION.
DOI=10.1002/(SICI)1097-0061(199907)15:10A<879::AID-YEA428>3.3.CO;2-H; PubMed=10407268 [NCBI, ExPASy, EBI, Israel, Japan]
Garay-Arroyo A., Covarrubias A.A.;
"Three genes whose expression is induced by stress in Saccharomyces cerevisiae.";
Yeast 15:879-892(1999).
[3]
 ACTIVITY ON METHYLGLYOXAL, AND INDUCTION.
DOI=10.1007/s002940100213; PubMed=11525399 [NCBI, ExPASy, EBI, Israel, Japan]
Aguilera J., Prieto J.A.;
"The Saccharomyces cerevisiae aldose reductase is implied in the metabolism of methylglyoxal in response to stress conditions.";
Curr. Genet. 39:273-283(2001).
[4]
 ACTIVITY ON XYLOSE.
DOI=10.1128/AEM.67.12.5668-5674.2001; PubMed=11722921 [NCBI, ExPASy, EBI, Israel, Japan]
Traff K.L., Otero Cordero R.R., van Zyl W.H., Hahn-Hagerdal B.;
"Deletion of the GRE3 aldose reductase gene and its influence on xylose metabolism in recombinant strains of Saccharomyces cerevisiae expressing the xylA and XKS1 genes.";
Appl. Environ. Microbiol. 67:5668-5674(2001).
[5]
 REVIEW, AND XYLOSE UTILIZATION.
DOI=10.1002/(SICI)1097-0061(199808)14:11<977::AID-YEA302>3.0.CO;2-J; PubMed=9730277 [NCBI, ExPASy, EBI, Israel, Japan]
Lee H.;
"The structure and function of yeast xylose (aldose) reductases.";
Yeast 14:977-984(1998).
[6]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: Reduces the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde similar to GRE2. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction.
  • CATALYTIC ACTIVITY: Alditol + NAD(P)+ = aldose + NAD(P)H.
  • CATALYTIC ACTIVITY: (R)-lactaldehyde + NADP+ = methylglyoxal + NADPH.
  • INTERACTION:
    P39079:CCT6; NbExp=1; IntAct=EBI-7884, EBI-19077;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • INDUCTION: By osmotic, ionic, oxidative and heat stress.
  • MISCELLANEOUS: Present with 12851 molecules/cell in log phase SD medium.
  • MISCELLANEOUS: 'De respuesta a estres' means stress response in Spanish.
  • SIMILARITY: Belongs to the aldo/keto reductase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U00059; AAB68858.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48946; S48946.
RefSeq NP_011972.1; -.
3D structure databases
HSSP O74237; 1K8C. [HSSP ENTRY / PDB]
ModBase P38715.
Protein-protein interaction databases
IntAct P38715; -.
Organism-specific databases
CYGD YHR104w; -.
SGD S000001146; GRE3.
Yeast-GFP YHR104W.
Gene expression databases
GermOnline YHR104W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0004032; Molecular function: aldehyde reductase activity (inferred from direct assay from SGD).
GO:0047935; Molecular function: glucose 1-dehydrogenase (NADP+) activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0019568; Biological process: arabinose catabolic process (inferred from direct assay from SGD).
GO:0042843; Biological process: D-xylose catabolic process (inferred from direct assay from SGD).
GO:0006979; Biological process: response to oxidative stress (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
BLOCKS P38715.
Proteomic databases
PeptideAtlas P38715; -.
Genome annotation databases
Ensembl YHR104W; Saccharomyces cerevisiae. [Contig view]
GeneID 856504; -.
GenomeReviews U00093_GR; YHR104W.
KEGG sce:YHR104W; -.
NMPDR fig|4932.3.peg.3133; -.
Phylogenomic databases
HOGENOM P38715; -.
Other
LinkHub P38715; -.
ProtoNet P38715.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NADP; Nucleus; Oxidoreductase; Phosphoprotein; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   327  327     NADPH-dependent aldose reductase GRE3. PRO_0000124678
NP_BIND   219   286  68     NADP (By similarity). 
ACT_SITE   49    49        Proton donor (By similarity). 
BINDING   111   111        Substrate (By similarity). 
SITE   78    78  1     Lowers pKa of active site Tyr (By similarity). 
MOD_RES   294   294        Phosphothreonine. 
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 37119 Da [This is the MW of the unprocessed precursor] CRC64: AFE72B8E2DFB91C8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSSLVTLNNG LKMPLVGLGC WKIDKKVCAN QIYEAIKLGY RLFDGACDYG NEKEVGEGIR 

        70         80         90        100        110        120 
KAISEGLVSR KDIFVVSKLW NNFHHPDHVK LALKKTLSDM GLDYLDLYYI HFPIAFKYVP 

       130        140        150        160        170        180 
FEEKYPPGFY TGADDEKKGH ITEAHVPIID TYRALEECVD EGLIKSIGVS NFQGSLIQDL 

       190        200        210        220        230        240 
LRGCRIKPVA LQIEHHPYLT QEHLVEFCKL HDIQVVAYSS FGPQSFIEMD LQLAKTTPTL 

       250        260        270        280        290        300 
FENDVIKKVS QNHPGSTTSQ VLLRWATQRG IAVIPKSSKK ERLLGNLEIE KKFTLTEQEL 

       310        320 
KDISALNANI RFNDPWTWLD GKFPTFA
P38715 in FASTA format

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