NADPH-dependent aldose reductase GRE3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38715 (GRE3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Nucleus
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-xylose catabolic process Inferred from mutant phenotype PubMed 12271459. Source: SGD arabinose catabolic process Inferred from mutant phenotype PubMed 12271459. Source: SGD cellular response to oxidative stress Inferred from genetic interaction PubMed 17919749. Source: SGD galactose catabolic process Inferred from genetic interaction PubMed 18811659. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: SGD nucleus Inferred from direct assay Ref.7. Source: SGD
Molecular_function	D-xylose:NADP reductase activity Inferred from mutant phenotype PubMed 11481678. Source: SGD glucose 1-dehydrogenase (NADP+) activity Inferred from direct assay PubMed 11306085. Source: SGD mRNA binding Inferred from direct assay PubMed 21124907. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 327

327

NADPH-dependent aldose reductase GRE3

PRO_0000124678

Regions

Nucleotide binding

219 – 286

NADP By similarity

Sites

Active site

Proton donor By similarity

Binding site

111

Substrate By similarity

Site

Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue

294

Phosphothreonine Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

P38715 [UniParc].

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

327

37,119

        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' referencesShow '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. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00059 Genomic DNA. Translation: AAB68858.1. BK006934 Genomic DNA. Translation: DAA06798.1.
PIR	S48946.
RefSeq	NP_011972.1. NM_001179234.1.
3D structure databases
ProteinModelPortal	P38715.
SMR	P38715. Positions 5-318.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38715. 2 interactions.
MINT	MINT-2784158.
STRING	4932.YHR104W.
Proteomic databases
PaxDb	P38715.
PeptideAtlas	P38715.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR104W; YHR104W; YHR104W.
GeneID	856504.
KEGG	sce:YHR104W.
Organism-specific databases
CYGD	YHR104w.
SGD	S000001146. GRE3.
Phylogenomic databases
eggNOG	COG0656.
GeneTree	ENSGT00550000074107.
HOGENOM	HOG000250272.
KO	K00011.
OMA	HITEAHV.
OrthoDB	EOG47SWPM.
Gene expression databases
Genevestigator	P38715.
GermOnline	YHR104W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.20.100. 1 hit.
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. IPR020471. Aldo/keto_reductase_subgr. IPR023210. NADP_OxRdtase_dom. [Graphical view]
PANTHER	PTHR11732. PTHR11732. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
PIRSF	PIRSF000097. AKR. 1 hit.
PRINTS	PR00069. ALDKETRDTASE.
SUPFAM	SSF51430. Aldo/ket_red. 1 hit.
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982230.

Entry information

Entry name

GRE3_YEAST

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents