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P38715 (GRE3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH-dependent aldose reductase GRE3

EC=1.1.1.21
Alternative name(s):
Genes de respuesta a estres protein 3
NADPH-dependent aldo-keto reductase GRE3
NADPH-dependent methylglyoxal reductase GRE3
Xylose reductase
EC=1.1.1.-
Gene names
Name:GRE3
Ordered Locus Names:YHR104W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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.

(R)-lactaldehyde + NADP+ = methylglyoxal + NADPH.

Subcellular location

Cytoplasm. Nucleus Ref.7.

Induction

By osmotic, ionic, oxidative and heat stress. Ref.3 Ref.4

Miscellaneous

Present with 12851 molecules/cell in log phase SD medium.

'De respuesta a estres' means stress response in Spanish.

Sequence similarities

Belongs to the aldo/keto reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327NADPH-dependent aldose reductase GRE3
PRO_0000124678

Regions

Nucleotide binding219 – 28668NADP By similarity

Sites

Active site491Proton donor By similarity
Binding site1111Substrate By similarity
Site781Lowers pKa of active site Tyr By similarity

Sequences

Sequence LengthMass (Da)Tools
P38715 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: AFE72B8E2DFB91C8

FASTA32737,119
        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 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
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. expand/collapse author list , 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.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Three genes whose expression is induced by stress in Saccharomyces cerevisiae."
Garay-Arroyo A., Covarrubias A.A.
Yeast 15:879-892(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[4]"The Saccharomyces cerevisiae aldose reductase is implied in the metabolism of methylglyoxal in response to stress conditions."
Aguilera J., Prieto J.A.
Curr. Genet. 39:273-283(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVITY ON METHYLGLYOXAL, INDUCTION.
[5]"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."
Traff K.L., Otero Cordero R.R., van Zyl W.H., Hahn-Hagerdal B.
Appl. Environ. Microbiol. 67:5668-5674(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVITY ON XYLOSE.
[6]"The structure and function of yeast xylose (aldose) reductases."
Lee H.
Yeast 14:977-984(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, XYLOSE UTILIZATION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00059 Genomic DNA. Translation: AAB68858.1.
BK006934 Genomic DNA. Translation: DAA06798.1.
PIRS48946.
RefSeqNP_011972.1. NM_001179234.1.

3D structure databases

ProteinModelPortalP38715.
SMRP38715. Positions 5-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36537. 130 interactions.
IntActP38715. 2 interactions.
MINTMINT-2784158.
STRING4932.YHR104W.

Proteomic databases

MaxQBP38715.
PaxDbP38715.
PeptideAtlasP38715.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR104W; YHR104W; YHR104W.
GeneID856504.
KEGGsce:YHR104W.

Organism-specific databases

CYGDYHR104w.
SGDS000001146. GRE3.

Phylogenomic databases

eggNOGCOG0656.
GeneTreeENSGT00750000117547.
HOGENOMHOG000250272.
KOK17743.
OMAHITEAHV.
OrthoDBEOG7WQ83S.

Enzyme and pathway databases

BioCycYEAST:YHR104W-MONOMER.

Gene expression databases

GenevestigatorP38715.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982230.

Entry information

Entry nameGRE3_YEAST
AccessionPrimary (citable) accession number: P38715
Secondary accession number(s): D3DL54
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families