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Protein

Glutathione S-transferase omega-like 2

Gene

ECM4

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

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). May be involved in cell wall organization and biogenesis.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=1.42 mM for reduced glutathione (GSH)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461Nucleophile1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • cell wall organization Source: UniProtKB-KW
    • glutathione metabolic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32040-MONOMER.
    SABIO-RKP36156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase omega-like 2 (EC:2.5.1.18)
    Alternative name(s):
    Extracellular mutant protein 4
    Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
    Gene namesi
    Name:ECM4
    Synonyms:GTO2
    Ordered Locus Names:YKR076W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XI

    Organism-specific databases

    CYGDiYKR076w.
    EuPathDBiFungiDB:YKR076W.
    SGDiS000001784. ECM4.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461C → S or Y: Completely inactive as thiol transferase. No activity recovered against 1-chloro-2,4-dinitrobenzene (CDNB). 1 Publication
    Mutagenesisi51 – 511R → A: No effect on thiol transferase activity. No effect on thiol transferase activity; when associated with D-173. 1 Publication
    Mutagenesisi173 – 1731E → A or D: No effect on thiol transferase activity. 1 Publication
    Mutagenesisi174 – 1741S → A: No effect on thiol transferase activity. 1 Publication
    Mutagenesisi246 – 2461L → A: No effect on thiol transferase activity. 1 Publication
    Mutagenesisi280 – 2801G → L: No effect on thiol transferase activity. 1 Publication
    Mutagenesisi287 – 2871D → G: Abolishes thiol transferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Glutathione S-transferase omega-like 2PRO_0000086922Add
    BLAST

    Proteomic databases

    MaxQBiP36156.
    PaxDbiP36156.
    PeptideAtlasiP36156.

    Expressioni

    Inductioni

    Under oxidative stress conditions. By agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide (t-BOOH) and cadmium in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.2 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi34207. 8 interactions.
    MINTiMINT-4493799.

    Structurei

    3D structure databases

    ProteinModelPortaliP36156.
    SMRiP36156. Positions 10-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini201 – 353153GST C-terminalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GST superfamily. Omega family.Curated
    Contains 1 GST C-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0435.
    GeneTreeiENSGT00530000065151.
    HOGENOMiHOG000245143.
    InParanoidiP36156.
    KOiK07393.
    OMAiETTNFEH.
    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.
    PROSITEiPS50405. GST_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P36156-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKQWASGTN GAFKRQVSSF RETISKQHPI YKPAKGRYWL YVSLACPWAH
    60 70 80 90 100
    RTLITRALKG LTSVIGCSVV HWHLDEKGWR FLDMEKQLED SEDFLEHWHD
    110 120 130 140 150
    VAGGIRTAKE DSSKSFAEIK NDSQRFMVDA TNEPHYGYKR ISDLYYKSDP
    160 170 180 190 200
    QYSARFTVPV LWDLETQTIV NNESSEIIRI LNSSAFDEFV DDDHKKTDLV
    210 220 230 240 250
    PAQLKTQIDD FNSWVYDSIN NGVYKTGFAE KAEVYESEVN NVFEHLDKVE
    260 270 280 290 300
    KILSDKYSKL KAKYGEEDRQ KILGEFFTVG DQLTEADIRL YTTVIRFDPV
    310 320 330 340 350
    YVQHFKCNFT SIRAGYPFIH LWVRNLYWNY DAFRYTTDFD HIKLHYTRSH
    360 370
    TRINPLGITP LGPKPDIRPL
    Length:370
    Mass (Da):43,274
    Last modified:June 1, 1994 - v1
    Checksum:i2ED6659ADD4CA6ED
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z28301 Genomic DNA. Translation: CAA82155.1.
    BK006944 Genomic DNA. Translation: DAA09226.1.
    PIRiS38153.
    RefSeqiNP_013002.3. NM_001179866.3.

    Genome annotation databases

    EnsemblFungiiYKR076W; YKR076W; YKR076W.
    GeneIDi853951.
    KEGGisce:YKR076W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z28301 Genomic DNA. Translation: CAA82155.1.
    BK006944 Genomic DNA. Translation: DAA09226.1.
    PIRiS38153.
    RefSeqiNP_013002.3. NM_001179866.3.

    3D structure databases

    ProteinModelPortaliP36156.
    SMRiP36156. Positions 10-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi34207. 8 interactions.
    MINTiMINT-4493799.

    Proteomic databases

    MaxQBiP36156.
    PaxDbiP36156.
    PeptideAtlasiP36156.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYKR076W; YKR076W; YKR076W.
    GeneIDi853951.
    KEGGisce:YKR076W.

    Organism-specific databases

    CYGDiYKR076w.
    EuPathDBiFungiDB:YKR076W.
    SGDiS000001784. ECM4.

    Phylogenomic databases

    eggNOGiCOG0435.
    GeneTreeiENSGT00530000065151.
    HOGENOMiHOG000245143.
    InParanoidiP36156.
    KOiK07393.
    OMAiETTNFEH.
    OrthoDBiEOG722JK6.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32040-MONOMER.
    SABIO-RKP36156.

    Miscellaneous databases

    NextBioi975356.
    PROiP36156.

    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.
    PROSITEiPS50405. GST_CTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
      Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
      Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MUTAGENESIS OF CYS-46; ARG-51; GLU-173; SER-174; LEU-246; GLY-280 AND ASP-287.
    7. "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: SUBCELLULAR LOCATION, INDUCTION.

    Entry informationi

    Entry nameiGTO2_YEAST
    AccessioniPrimary (citable) accession number: P36156
    Secondary accession number(s): D6VXD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: July 22, 2015
    This is version 121 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 1670 molecules/cell in log phase SD medium.1 Publication
    A version of this protein truncated after amino acid 200 is not active in the beta-hydroxyethyl disulfide (HED) assay.

    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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: 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.