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Protein

NADPH-dependent methylglyoxal reductase GRE2

Gene

GRE2

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

Functioni

Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. 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. Also catalyzes the reduction of 3-methylbutanal to 3-methylbutanol. Acts as a suppressor of 3-methylbutanol-induced filamentation by modulating the levels of 3-methylbutanal, the signal to which cells respond by filamentation. Also involved in ergosterol metabolism.4 Publications

Miscellaneous

Present with 5458 molecules/cell in log phase SD medium.1 Publication
'De respuesta a estres' means stress response in Spanish.

Catalytic activityi

(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH.3 Publications
3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H.1 Publication

Enzyme regulationi

Activated by glutathione.

Kineticsi

kcat is 31.3 min(-1) with 3-chloro-1-phenyl-1-propanol as substrate and 29.1 min(-1) for NADPH.
  1. KM=5.88 mM for methylglyoxal1 Publication
  2. KM=1.54 mM for phenylglyoxal1 Publication
  3. KM=0.14 mM for 3-methylbutanal1 Publication
  4. KM=0.192 mM for 3-chloro-1-phenyl-1-propanol2 Publications
  5. KM=4.33 mM for 2,5-hexanedione2 Publications
  6. KM=10.48 mM for (2S,5S)-hexanediol2 Publications
  7. KM=0.112 mM for NADPH2 Publications

    pH dependencei

    Optimum pH is 7 for 2,5-hexanedione reduction, and 10 for the reverse reaction.2 Publications

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius for 3-chloro-1-phenyl-1-propanol reduction, and 54 degrees Celsius for 2,5-hexanedione reduction, and 30 degrees Celsius for the reverse reaction.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei32NADP1 Publication1
    Binding sitei36NADP1 Publication1
    Binding sitei165NADP1 Publication1
    Active sitei169Proton donor1 Publication1
    Binding sitei169NADP1 Publication1
    Binding sitei199NADP; via amide nitrogen1 Publication1
    Binding sitei216NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi7 – 12NADP1 Publication6
    Nucleotide bindingi57 – 58NADP1 Publication2

    GO - Molecular functioni

    • 3-beta-hydroxy-delta5-steroid dehydrogenase activity Source: InterPro
    • 3-methylbutanol:NAD(P) oxidoreductase activity Source: SGD
    • methylglyoxal reductase (NADPH-dependent) activity Source: SGD

    GO - Biological processi

    • ergosterol metabolic process Source: SGD
    • filamentous growth Source: SGD
    • steroid biosynthetic process Source: InterPro

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyciMetaCyc:YOL151W-MONOMER
    YEAST:YOL151W-MONOMER
    SABIO-RKQ12068

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent methylglyoxal reductase GRE2 (EC:1.1.1.2833 Publications)
    Alternative name(s):
    3-methylbutanal reductase (EC:1.1.1.2651 Publication)
    Genes de respuesta a estres protein 2
    Isovaleraldehyde reductase
    Gene namesi
    Name:GRE2
    Ordered Locus Names:YOL151W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XV

    Organism-specific databases

    EuPathDBiFungiDB:YOL151W
    SGDiS000005511 GRE2

    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

    Pathology & Biotechi

    Biotechnological usei

    Used as a biocatalyst, because the enzyme accepts a broad range of substrates including aliphatic and aromatic ketones, chloroketones, diketones as well as beta-ketoesters which are reduced with high stereoselectivity.2 Publications

    Disruption phenotypei

    Causes hyperfilamentation, probably due to the elevated levels of 3-methylbutanal in the mutant.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi9N → E: Alters cofactor preference of the enzyme to be able to use as well NAD instead of NADP. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002155761 – 342NADPH-dependent methylglyoxal reductase GRE2Add BLAST342

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei333PhosphoserineCombined sources1

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12068
    PaxDbiQ12068
    PRIDEiQ12068

    PTM databases

    iPTMnetiQ12068

    Expressioni

    Inductioni

    Repressed by SKO1. During osmotic stress, this repression is relieved. Induced by transcription factor YAP1 during oxidative stress, and induced by ionic and heat stress. Induced by isoamylalcohol.4 Publications

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi34267, 56 interactors
    DIPiDIP-2645N
    IntActiQ12068, 1 interactor
    MINTiQ12068
    STRINGi4932.YOL151W

    Structurei

    Secondary structure

    1342
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 6Combined sources4
    Turni7 – 9Combined sources3
    Helixi11 – 22Combined sources12
    Beta strandi27 – 33Combined sources7
    Helixi34 – 43Combined sources10
    Beta strandi50 – 54Combined sources5
    Turni61 – 64Combined sources4
    Helixi65 – 71Combined sources7
    Turni72 – 74Combined sources3
    Beta strandi77 – 80Combined sources4
    Beta strandi89 – 91Combined sources3
    Helixi92 – 95Combined sources4
    Helixi97 – 114Combined sources18
    Turni116 – 118Combined sources3
    Beta strandi121 – 125Combined sources5
    Helixi128 – 130Combined sources3
    Helixi134 – 136Combined sources3
    Beta strandi143 – 145Combined sources3
    Helixi156 – 159Combined sources4
    Helixi161 – 182Combined sources22
    Turni183 – 186Combined sources4
    Beta strandi190 – 196Combined sources7
    Beta strandi198 – 201Combined sources4
    Helixi206 – 210Combined sources5
    Helixi215 – 224Combined sources10
    Beta strandi236 – 241Combined sources6
    Helixi242 – 254Combined sources13
    Turni257 – 260Combined sources4
    Beta strandi262 – 265Combined sources4
    Beta strandi268 – 271Combined sources4
    Helixi272 – 282Combined sources11
    Turni284 – 289Combined sources6
    Turni299 – 301Combined sources3
    Beta strandi307 – 309Combined sources3
    Helixi311 – 317Combined sources7
    Helixi324 – 338Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4PVCX-ray2.00A/B1-342[»]
    4PVDX-ray2.40A/B/C/D1-342[»]
    ProteinModelPortaliQ12068
    SMRiQ12068
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00390000002618
    HOGENOMiHOG000167998
    InParanoidiQ12068
    KOiK17741
    OMAiTHDEVCK
    OrthoDBiEOG092C3RD2

    Family and domain databases

    InterProiView protein in InterPro
    IPR002225 3Beta_OHSteriod_DH/Estase
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF01073 3Beta_HSD, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q12068-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSVFVSGANG FIAQHIVDLL LKEDYKVIGS ARSQEKAENL TEAFGNNPKF
    60 70 80 90 100
    SMEVVPDISK LDAFDHVFQK HGKDIKIVLH TASPFCFDIT DSERDLLIPA
    110 120 130 140 150
    VNGVKGILHS IKKYAADSVE RVVLTSSYAA VFDMAKENDK SLTFNEESWN
    160 170 180 190 200
    PATWESCQSD PVNAYCGSKK FAEKAAWEFL EENRDSVKFE LTAVNPVYVF
    210 220 230 240 250
    GPQMFDKDVK KHLNTSCELV NSLMHLSPED KIPELFGGYI DVRDVAKAHL
    260 270 280 290 300
    VAFQKRETIG QRLIVSEARF TMQDVLDILN EDFPVLKGNI PVGKPGSGAT
    310 320 330 340
    HNTLGATLDN KKSKKLLGFK FRNLKETIDD TASQILKFEG RI
    Length:342
    Mass (Da):38,170
    Last modified:November 1, 1996 - v1
    Checksum:i84DC286AAD8C88D2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z48239 Genomic DNA Translation: CAA88277.1
    Z74893 Genomic DNA Translation: CAA99172.1
    AY558040 Genomic DNA Translation: AAS56366.1
    BK006948 Genomic DNA Translation: DAA10635.1
    PIRiS60386
    RefSeqiNP_014490.1, NM_001183405.1

    Genome annotation databases

    EnsemblFungiiYOL151W; YOL151W; YOL151W
    GeneIDi854014
    KEGGisce:YOL151W

    Similar proteinsi

    Entry informationi

    Entry nameiGRE2_YEAST
    AccessioniPrimary (citable) accession number: Q12068
    Secondary accession number(s): D6W1R9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2004
    Last sequence update: November 1, 1996
    Last modified: May 23, 2018
    This is version 138 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

    3D-structure, Complete proteome, Reference proteome

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