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Protein

Glutathione S-transferase GstA

Gene

gstA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.4 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.3 Publications

Kineticsi

kcat is 9 sec(-1) for the GSH transferase reaction with CDNB as substrate.1 Publication

  1. KM=0.041 mM for glutathione3 Publications
  2. KM=0.3 mM for glutathione3 Publications
  3. KM=0.99 mM for 1-chloro-2,4-dinitrobenzene3 Publications
  4. KM=1.9 mM for 1-chloro-2,4-dinitrobenzene3 Publications

    pH dependencei

    Optimum pH is 7.5.2 Publications

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Glutathione
    Binding sitei35 – 351Glutathione
    Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen
    Binding sitei99 – 991Glutathione

    GO - Molecular functioni

    • glutathione transferase activity Source: EcoCyc

    GO - Biological processi

    • xenobiotic catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:GST-MONOMER.
    ECOL316407:JW1627-MONOMER.
    MetaCyc:GST-MONOMER.
    RETL1328306-WGS:GSTH-1203-MONOMER.
    BRENDAi2.5.1.18. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase GstA (EC:2.5.1.18)
    Alternative name(s):
    GST B1-1
    Gene namesi
    Name:gstA
    Synonyms:gst
    Ordered Locus Names:b1635, JW1627
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12613. gstA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Deletion of the gstA gene decreases the resistance of the bacteria to hydrogen peroxide.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51Y → F: Does not significantly affect the activity. 1 Publication
    Mutagenesisi10 – 101C → A: 8-fold decrease in affinity for GSH, but 5-fold increase in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. 1 Publication
    Mutagenesisi10 – 101C → S: 6-fold decrease in affinity for GSH, and decrease in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. 1 Publication
    Mutagenesisi106 – 1061H → A: Decrease in affinity for GSH while nearly no effect on affinity for CDNB, and decrease in GSH transferase activity. 1 Publication
    Mutagenesisi106 – 1061H → F: Decrease in affinity for GSH, while nearly no effect on affinity for CDNB and on GSH transferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Glutathione S-transferase GstAPRO_0000185970Add
    BLAST

    Proteomic databases

    PaxDbiP0A9D2.
    PRIDEiP0A9D2.

    2D gel databases

    SWISS-2DPAGEP0A9D2.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    DIPiDIP-9851N.
    IntActiP0A9D2. 1 interaction.
    STRINGi511145.b1635.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54Combined sources
    Helixi12 – 209Combined sources
    Beta strandi26 – 316Combined sources
    Turni32 – 354Combined sources
    Helixi43 – 453Combined sources
    Beta strandi54 – 563Combined sources
    Beta strandi62 – 654Combined sources
    Helixi66 – 7510Combined sources
    Helixi78 – 803Combined sources
    Helixi89 – 10416Combined sources
    Helixi106 – 1138Combined sources
    Beta strandi115 – 1173Combined sources
    Helixi119 – 1213Combined sources
    Helixi122 – 13918Combined sources
    Turni140 – 1423Combined sources
    Beta strandi143 – 1453Combined sources
    Beta strandi146 – 1505Combined sources
    Helixi153 – 16715Combined sources
    Helixi176 – 18611Combined sources
    Helixi189 – 1979Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A0FX-ray2.10A/B1-201[»]
    1N2AX-ray1.90A/B1-201[»]
    ProteinModelPortaliP0A9D2.
    SMRiP0A9D2. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9D2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8181GST N-terminalAdd
    BLAST
    Domaini87 – 201115GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 662Glutathione binding
    Regioni103 – 1064Glutathione binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125748.
    InParanoidiP0A9D2.
    KOiK00799.
    OMAiSHKLQDG.
    OrthoDBiEOG6H1Q01.
    PhylomeDBiP0A9D2.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9D2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DDYFAVNPKG
    60 70 80 90 100
    QVPALLLDDG TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY
    110 120 130 140 150
    IATELHKGFT PLFRPDTPEE YKPTVRAQLE KKLQYVNEAL KDEHWICGQR
    160 170 180 190 200
    FTIADAYLFT VLRWAYAVKL NLEGLEHIAA FMQRMAERPE VQDALSAEGL

    K
    Length:201
    Mass (Da):22,868
    Last modified:July 19, 2005 - v1
    Checksum:i6347401123B044E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21K → L AA sequence (PubMed:2185038).Curated
    Sequence conflicti5 – 62YK → IL AA sequence (PubMed:2185038).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D38497 Genomic DNA. Translation: BAA07509.1.
    U00096 Genomic DNA. Translation: AAC74707.1.
    AP009048 Genomic DNA. Translation: BAA15396.1.
    PIRiA55495.
    RefSeqiNP_416152.1. NC_000913.3.
    WP_000765749.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74707; AAC74707; b1635.
    BAA15396; BAA15396; BAA15396.
    GeneIDi945758.
    KEGGieco:b1635.
    PATRICi32118572. VBIEscCol129921_1706.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D38497 Genomic DNA. Translation: BAA07509.1.
    U00096 Genomic DNA. Translation: AAC74707.1.
    AP009048 Genomic DNA. Translation: BAA15396.1.
    PIRiA55495.
    RefSeqiNP_416152.1. NC_000913.3.
    WP_000765749.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A0FX-ray2.10A/B1-201[»]
    1N2AX-ray1.90A/B1-201[»]
    ProteinModelPortaliP0A9D2.
    SMRiP0A9D2. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-9851N.
    IntActiP0A9D2. 1 interaction.
    STRINGi511145.b1635.

    2D gel databases

    SWISS-2DPAGEP0A9D2.

    Proteomic databases

    PaxDbiP0A9D2.
    PRIDEiP0A9D2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74707; AAC74707; b1635.
    BAA15396; BAA15396; BAA15396.
    GeneIDi945758.
    KEGGieco:b1635.
    PATRICi32118572. VBIEscCol129921_1706.

    Organism-specific databases

    EchoBASEiEB2497.
    EcoGeneiEG12613. gstA.

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125748.
    InParanoidiP0A9D2.
    KOiK00799.
    OMAiSHKLQDG.
    OrthoDBiEOG6H1Q01.
    PhylomeDBiP0A9D2.

    Enzyme and pathway databases

    BioCyciEcoCyc:GST-MONOMER.
    ECOL316407:JW1627-MONOMER.
    MetaCyc:GST-MONOMER.
    RETL1328306-WGS:GSTH-1203-MONOMER.
    BRENDAi2.5.1.18. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A9D2.
    PROiP0A9D2.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli. The conserved tyrosyl residue near the N-terminus is not essential for catalysis."
      Nishida M., Kong K.-H., Inoue H., Takahashi K.
      J. Biol. Chem. 269:32536-32541(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF TYR-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Purification and study of a bacterial glutathione S-transferase."
      Arca P., Garcia P., Hardisson C., Suarez J.E.
      FEBS Lett. 263:77-79(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: K12.
    6. "Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress."
      Kanai T., Takahashi K., Inoue H.
      J. Biochem. 140:703-711(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, DISRUPTION PHENOTYPE.
      Strain: K12.
    7. "Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys(10) and His(106)."
      Wang X.Y., Zhang Z.R., Perrett S.
      Biochem. J. 417:55-64(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-10 AND HIS-106.
    8. "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106."
      Nishida M., Harada S., Noguchi S., Satow Y., Inoue H., Takahashi K.
      J. Mol. Biol. 281:135-147(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE SULFONATE, SUBUNIT.
    9. "Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli."
      Rife C.L., Parsons J.F., Xiao G., Gilliland G.L., Armstrong R.N.
      Proteins 53:777-782(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE SULFONATE, SUBUNIT.

    Entry informationi

    Entry nameiGSTA_ECOLI
    AccessioniPrimary (citable) accession number: P0A9D2
    Secondary accession number(s): P39100
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: July 22, 2015
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    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.