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Protein

Glutathione S-transferase omega-like 1

Gene

GTO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB).1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.1 Publication

Kineticsi

  1. KM=1.13 mM for reduced glutathione (GSH)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei31 – 311NucleophileBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • glutathione metabolic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30856-MONOMER.
    SABIO-RKP48239.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase omega-like 1 (EC:2.5.1.18)
    Alternative name(s):
    Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
    Gene namesi
    Name:GTO1
    Ordered Locus Names:YGR154C
    ORF Names:G6664
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome VII

    Organism-specific databases

    CYGDiYGR154c.
    EuPathDBiFungiDB:YGR154C.
    SGDiS000003386. GTO1.

    Subcellular locationi

    GO - Cellular componenti

    • peroxisome Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Disruption phenotypei

    Null mutants display increased sensitivity to cadmium in the absence of GTT1 and GTT2. Null mutants also show growth defects on oleic acid-based medium, indicative of abnormal peroxisomal functions and altered expression of genes related to sulfur amino acid metabolism, and have low levels of reduced glutathione.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356Glutathione S-transferase omega-like 1PRO_0000202833Add
    BLAST

    Proteomic databases

    PaxDbiP48239.

    Expressioni

    Inductioni

    By diamide and 1-chloro-2,4-dinitrobenzene (CDNB) in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi33402. 7 interactions.
    DIPiDIP-1867N.
    IntActiP48239. 1 interaction.
    MINTiMINT-392461.

    Structurei

    3D structure databases

    ProteinModelPortaliP48239.
    SMRiP48239. Positions 16-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili214 – 25744Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GST superfamily. Omega family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0435.
    GeneTreeiENSGT00530000065151.
    HOGENOMiHOG000245143.
    InParanoidiP48239.
    OMAiNNSADIM.
    OrthoDBiEOG722JK6.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 2 hits.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR016639. GST.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR32419. PTHR32419. 1 hit.
    PfamiPF13409. GST_N_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015753. GST. 1 hit.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P48239-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSVSYKGTIS KTHSVFKPEK GRYYIYGALG CPFTHRAILA RSLKKLEPVL
    60 70 80 90 100
    GLVLSHWQLD SKGARFLPAP HRPEKYKERF FTATGGIASA KLDESEELGD
    110 120 130 140 150
    VNNDSARLFV DGAFDPVENI SRLSELYYLN DPKYPGTKFT VPVLWDSKTR
    160 170 180 190 200
    KIVNNESGDI IRILNSGVFD EFIQSEETNV IDLVPHDLID EIDKNIKWVH
    210 220 230 240 250
    PKINLGVYKV GLAENGKIYE TEVKTLFENL QKMECVLKEN YKRLEEQFSG
    260 270 280 290 300
    NKQKILAKYF VLGQRLTEAD IRLYPSIIRF DVVYVQHFKC NLKTIRDGFP
    310 320 330 340 350
    YLHLWLINLY WNYAEFRFTT DFNHIKLFYI RMEVSRNKIN QFGIVPLGPK

    PDISRL
    Length:356
    Mass (Da):41,301
    Last modified:February 1, 1996 - v1
    Checksum:iB4639BD195CDF7F5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X85807 Genomic DNA. Translation: CAA59811.1.
    Z72939 Genomic DNA. Translation: CAA97168.1.
    BK006941 Genomic DNA. Translation: DAA08245.1.
    PIRiS60444.
    RefSeqiNP_011670.3. NM_001181283.3.

    Genome annotation databases

    EnsemblFungiiYGR154C; YGR154C; YGR154C.
    GeneIDi853058.
    KEGGisce:YGR154C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X85807 Genomic DNA. Translation: CAA59811.1.
    Z72939 Genomic DNA. Translation: CAA97168.1.
    BK006941 Genomic DNA. Translation: DAA08245.1.
    PIRiS60444.
    RefSeqiNP_011670.3. NM_001181283.3.

    3D structure databases

    ProteinModelPortaliP48239.
    SMRiP48239. Positions 16-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33402. 7 interactions.
    DIPiDIP-1867N.
    IntActiP48239. 1 interaction.
    MINTiMINT-392461.

    Proteomic databases

    PaxDbiP48239.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR154C; YGR154C; YGR154C.
    GeneIDi853058.
    KEGGisce:YGR154C.

    Organism-specific databases

    CYGDiYGR154c.
    EuPathDBiFungiDB:YGR154C.
    SGDiS000003386. GTO1.

    Phylogenomic databases

    eggNOGiCOG0435.
    GeneTreeiENSGT00530000065151.
    HOGENOMiHOG000245143.
    InParanoidiP48239.
    OMAiNNSADIM.
    OrthoDBiEOG722JK6.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30856-MONOMER.
    SABIO-RKP48239.

    Miscellaneous databases

    NextBioi972989.
    PROiP48239.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 2 hits.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR016639. GST.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR32419. PTHR32419. 1 hit.
    PfamiPF13409. GST_N_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015753. GST. 1 hit.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
      Skala J., Nawrocki A., Goffeau A.
      Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases."
      Garcera A., Barreto L., Piedrafita L., Tamarit J., Herrero E.
      Biochem. J. 398:187-196(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism."
      Barreto L., Garcera A., Jansson K., Sunnerhagen P., Herrero E.
      Eukaryot. Cell 5:1748-1759(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION.

    Entry informationi

    Entry nameiGTO1_YEAST
    AccessioniPrimary (citable) accession number: P48239
    Secondary accession number(s): D6VUT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: July 22, 2015
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: 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.