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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: -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

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
    Active sitei49Proton donorBy similarity1
    Sitei78Lowers pKa of active site TyrBy similarity1
    Binding sitei111SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi219 – 286NADPBy similarityAdd BLAST68

    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

    Keywordsi

    Molecular functionOxidoreductase
    Biological processStress response
    LigandNADP

    Enzyme and pathway databases

    BioCyciYEAST:YHR104W-MONOMER

    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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001246782 – 327NADPH-dependent aldose reductase GRE3Add BLAST326

    Proteomic databases

    MaxQBiP38715
    PaxDbiP38715
    PRIDEiP38715

    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, 157 interactors
    IntActiP38715, 2 interactors
    MINTiP38715
    STRINGi4932.YHR104W

    Structurei

    3D structure databases

    ProteinModelPortaliP38715
    SMRiP38715
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00910000144337
    HOGENOMiHOG000250272
    InParanoidiP38715
    KOiK17743
    OMAiKIWTENL
    OrthoDBiEOG092C324N

    Family and domain databases

    CDDicd06660 Aldo_ket_red, 1 hit
    Gene3Di3.20.20.100, 1 hit
    InterProiView protein in InterPro
    IPR018170 Aldo/ket_reductase_CS
    IPR020471 Aldo/keto_reductase
    IPR023210 NADP_OxRdtase_dom
    IPR036812 NADP_OxRdtase_dom_sf
    PANTHERiPTHR11732 PTHR11732, 1 hit
    PfamiView protein in Pfam
    PF00248 Aldo_ket_red, 1 hit
    PIRSFiPIRSF000097 AKR, 1 hit
    PRINTSiPR00069 ALDKETRDTASE
    SUPFAMiSSF51430 SSF51430, 1 hit
    PROSITEiView protein in PROSITE
    PS00798 ALDOKETO_REDUCTASE_1, 1 hit
    PS00062 ALDOKETO_REDUCTASE_2, 1 hit
    PS00063 ALDOKETO_REDUCTASE_3, 1 hit

    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

    Similar proteinsi

    Entry informationi

    Entry nameiGRE3_YEAST
    AccessioniPrimary (citable) accession number: P38715
    Secondary accession number(s): D3DL54
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: May 23, 2018
    This is version 169 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

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