Reviewed, UniProtKB/Swiss-Prot P38715 (GRE3_YEAST)

Names and origin

Protein names

Recommended name:
    NADPH-dependent aldose reductase GRE3
    EC=1.1.1.21
Alternative name(s):
    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 names

Name:	GRE3
Ordered Locus Names:	YHR104W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Induction	By osmotic, ionic, oxidative and heat stress.
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
Gene Ontology (GO)
Biological process	D-xylose catabolic process Inferred from direct assay. Source: SGD arabinose catabolic process Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Ref.6 Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.6 Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aldehyde reductase activity Ref.3 Inferred from electronic annotation. Source: EC glucose 1-dehydrogenase (NADP+) activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCT6	P39079	1	EBI-7884,EBI-19077

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	68	NADP By similarity
Sites
	Active site	49	1	Proton donor By similarity
	Binding site	111	1	Substrate By similarity
	Site	78	1	Lowers pKa of active site Tyr By similarity
Amino acid modifications
	Modified residue	294	1	Phosphothreonine

Sequences

	Sequence		Length	Mass (Da)
	P38715-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: AFE72B8E2DFB91C8	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

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. , 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: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Three genes whose expression is induced by stress in Saccharomyces cerevisiae." Garay-Arroyo A., Covarrubias A.A. Yeast 15:879-892(1999) [PubMed: 10407268] [Abstract] Cited for: INDUCTION.
[3]	"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: 11525399] [Abstract] Cited for: ACTIVITY ON METHYLGLYOXAL, INDUCTION.
[4]	"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: 11722921] [Abstract] Cited for: ACTIVITY ON XYLOSE.
[5]	"The structure and function of yeast xylose (aldose) reductases." Lee H. Yeast 14:977-984(1998) [PubMed: 9730277] [Abstract] Cited for: REVIEW, XYLOSE UTILIZATION.
[6]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00059 Genomic DNA. Translation: AAB68858.1.
PIR	S48946.
RefSeq	NP_011972.1.
3D structure databases
HSSP	HSSP built from PDB template 1K8C based on UniProtKB O74237.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38715.
Proteomic databases
PeptideAtlas	P38715.
Genome annotation databases
Ensembl	YHR104W. Saccharomyces cerevisiae. [Contig view]
GeneID	856504.
GenomeReviews	Gene locus YHR104W in contig U00093_GR.
KEGG	sce:YHR104W.
NMPDR	fig|4932.3.peg.3133.
Organism-specific databases
CYGD	YHR104w.
SGD	S000001146. GRE3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38715.
Gene expression databases
GermOnline	YHR104W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
PRINTS	PR00069. ALDKETRDTASE.
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P38715.
NextBio	982230.

Entry information

Entry name

GRE3_YEAST

Accession

Primary (citable) accession number: P38715

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)