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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

Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)-lactaldehyde under stress conditions. 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 (PubMed:11525399). 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 (Probable) (PubMed:11722921).1 Publication3 Publications

Catalytic activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.2 Publications

Kineticsi

  1. KM=0.046 mM for p-nitrobenzaldehyde1 Publication
  2. KM=1.44 mM for D-L-glyceraldehyde1 Publication
  3. KM=1.57 mM for D-glyceraldehyde1 Publication
  4. KM=6.38 mM for L-glyceraldehyde1 Publication
  5. KM=27.9 mM for D-xylose1 Publication
  6. KM=32.63 mM for L-arabinose1 Publication
  7. KM=9.34 mM for D-glucose1 Publication
  8. KM=0.013 mM for NADPH1 Publication

    pH dependencei

    Optimum pH is 5.1 Publication

    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

    • alditol:NADP+ 1-oxidoreductase activity Source: SGD
    • D-xylose:NADP reductase activity Source: SGD
    • mRNA binding Source: SGD

    GO - Biological processi

    • arabinose catabolic process Source: SGD
    • cellular response to osmotic stress Source: SGD
    • cellular response to oxidative stress Source: SGD
    • D-xylose catabolic process Source: SGD
    • 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.
    ReactomeiR-SCE-156590. Glutathione conjugation.
    R-SCE-193144. Estrogen biosynthesis.
    R-SCE-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-SCE-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-SCE-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    R-SCE-196108. Pregnenolone biosynthesis.
    R-SCE-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    R-SCE-5365859. RA biosynthesis pathway.
    R-SCE-5652227. Fructose biosynthesis.
    R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent aldose reductase GRE31 Publication (EC:1.1.1.211 Publication)
    Short name:
    AR1 Publication
    Alternative name(s):
    Genes de respuesta a estres protein 31 Publication
    NADPH-dependent aldo-keto reductase GRE31 Publication
    Xylose reductase1 Publication (EC:1.1.1.-)
    Gene namesi
    Name:GRE31 Publication
    Ordered Locus Names:YHR104WImported
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VIII

    Organism-specific databases

    EuPathDBiFungiDB:YHR104W.
    SGDiS000001146. GRE3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 327326NADPH-dependent aldose reductase GRE3PRO_0000124678Add
    BLAST

    Proteomic databases

    MaxQBiP38715.
    PeptideAtlasiP38715.

    PTM databases

    iPTMnetiP38715.

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi36537. 130 interactions.
    IntActiP38715. 2 interactions.
    MINTiMINT-2784158.

    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

    GeneTreeiENSGT00830000129046.
    HOGENOMiHOG000250272.
    InParanoidiP38715.
    KOiK17743.
    OMAiFPIAFKY.
    OrthoDBiEOG7WQ83S.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    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:February 1, 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. 130 interactions.
    IntActiP38715. 2 interactions.
    MINTiMINT-2784158.

    PTM databases

    iPTMnetiP38715.

    Proteomic databases

    MaxQBiP38715.
    PeptideAtlasiP38715.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:YHR104W.
    SGDiS000001146. GRE3.

    Phylogenomic databases

    GeneTreeiENSGT00830000129046.
    HOGENOMiHOG000250272.
    InParanoidiP38715.
    KOiK17743.
    OMAiFPIAFKY.
    OrthoDBiEOG7WQ83S.

    Enzyme and pathway databases

    BioCyciYEAST:YHR104W-MONOMER.
    ReactomeiR-SCE-156590. Glutathione conjugation.
    R-SCE-193144. Estrogen biosynthesis.
    R-SCE-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-SCE-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-SCE-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    R-SCE-196108. Pregnenolone biosynthesis.
    R-SCE-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    R-SCE-5365859. RA biosynthesis pathway.
    R-SCE-5652227. Fructose biosynthesis.
    R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

    Miscellaneous databases

    NextBioi982230.
    PROiP38715.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    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. "Purification and partial characterization of an aldo-keto reductase from Saccharomyces cerevisiae."
      Kuhn A., van Zyl C., van Tonder A., Prior B.A.
      Appl. Environ. Microbiol. 61:1580-1585(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 26602.
    4. "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.
    5. "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: CATALYTIC ACTIVITY, ACTIVITY ON METHYLGLYOXAL, INDUCTION.
    6. "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.
    7. "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.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. 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: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: May 11, 2016
    This is version 152 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.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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

    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 one 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.