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Protein

NADPH-dependent aldose reductase GRE3

Gene

GRE3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.
(R)-lactaldehyde + NADP+ = methylglyoxal + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Proton donorBy similarity
Sitei78 – 781Lowers pKa of active site TyrBy similarity
Binding sitei111 – 1111SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi219 – 28668NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: SGD
  2. D-xylose:NADP reductase activity Source: SGD
  3. mRNA binding Source: SGD

GO - Biological processi

  1. arabinose catabolic process Source: SGD
  2. cellular response to osmotic stress Source: SGD
  3. cellular response to oxidative stress Source: SGD
  4. D-xylose catabolic process Source: SGD
  5. galactose catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:YHR104W-MONOMER.
ReactomeiREACT_290215. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_317578. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_335712. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_336636. Pregnenolone biosynthesis.
REACT_341789. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_344961. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GRE3
Ordered Locus Names:YHR104W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VIII

Organism-specific databases

CYGDiYHR104w.
SGDiS000001146. GRE3.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327NADPH-dependent aldose reductase GRE3PRO_0000124678Add
BLAST

Proteomic databases

MaxQBiP38715.
PaxDbiP38715.
PeptideAtlasiP38715.

Expressioni

Inductioni

By osmotic, ionic, oxidative and heat stress.2 Publications

Gene expression databases

GenevestigatoriP38715.

Interactioni

Protein-protein interaction databases

BioGridi36537. 131 interactions.
IntActiP38715. 2 interactions.
MINTiMINT-2784158.
STRINGi4932.YHR104W.

Structurei

3D structure databases

ProteinModelPortaliP38715.
SMRiP38715. Positions 5-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00780000122454.
HOGENOMiHOG000250272.
InParanoidiP38715.
KOiK17743.
OMAiHITEAHV.
OrthoDBiEOG7WQ83S.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLVTLNNG LKMPLVGLGC WKIDKKVCAN QIYEAIKLGY RLFDGACDYG
60 70 80 90 100
NEKEVGEGIR KAISEGLVSR KDIFVVSKLW NNFHHPDHVK LALKKTLSDM
110 120 130 140 150
GLDYLDLYYI HFPIAFKYVP FEEKYPPGFY TGADDEKKGH ITEAHVPIID
160 170 180 190 200
TYRALEECVD EGLIKSIGVS NFQGSLIQDL LRGCRIKPVA LQIEHHPYLT
210 220 230 240 250
QEHLVEFCKL HDIQVVAYSS FGPQSFIEMD LQLAKTTPTL FENDVIKKVS
260 270 280 290 300
QNHPGSTTSQ VLLRWATQRG IAVIPKSSKK ERLLGNLEIE KKFTLTEQEL
310 320
KDISALNANI RFNDPWTWLD GKFPTFA
Length:327
Mass (Da):37,119
Last modified:January 31, 1995 - v1
Checksum:iAFE72B8E2DFB91C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00059 Genomic DNA. Translation: AAB68858.1.
BK006934 Genomic DNA. Translation: DAA06798.1.
PIRiS48946.
RefSeqiNP_011972.1. NM_001179234.1.

Genome annotation databases

EnsemblFungiiYHR104W; YHR104W; YHR104W.
GeneIDi856504.
KEGGisce:YHR104W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00059 Genomic DNA. Translation: AAB68858.1.
BK006934 Genomic DNA. Translation: DAA06798.1.
PIRiS48946.
RefSeqiNP_011972.1. NM_001179234.1.

3D structure databases

ProteinModelPortaliP38715.
SMRiP38715. Positions 5-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36537. 131 interactions.
IntActiP38715. 2 interactions.
MINTiMINT-2784158.
STRINGi4932.YHR104W.

Proteomic databases

MaxQBiP38715.
PaxDbiP38715.
PeptideAtlasiP38715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR104W; YHR104W; YHR104W.
GeneIDi856504.
KEGGisce:YHR104W.

Organism-specific databases

CYGDiYHR104w.
SGDiS000001146. GRE3.

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00780000122454.
HOGENOMiHOG000250272.
InParanoidiP38715.
KOiK17743.
OMAiHITEAHV.
OrthoDBiEOG7WQ83S.

Enzyme and pathway databases

BioCyciYEAST:YHR104W-MONOMER.
ReactomeiREACT_290215. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_317578. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_335712. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_336636. Pregnenolone biosynthesis.
REACT_341789. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_344961. RA biosynthesis pathway.

Miscellaneous databases

NextBioi982230.

Gene expression databases

GenevestigatoriP38715.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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(1998) [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(2000) [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(2000) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, XYLOSE UTILIZATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGRE3_YEAST
AccessioniPrimary (citable) accession number: P38715
Secondary accession number(s): D3DL54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1995
Last sequence update: January 31, 1995
Last modified: March 31, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12851 molecules/cell in log phase SD medium.1 Publication
'De respuesta a estres' means stress response in Spanish.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.