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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Binding sitei10Glutathione1 Publication1
    Binding sitei35Glutathione1 Publication1
    Binding sitei52Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1
    Binding sitei99Glutathione1 Publication1

    GO - Molecular functioni

    • glutathione transferase activity Source: EcoCyc

    GO - Biological processi

    • glutathione metabolic process Source: GO_Central
    • response to hydrogen peroxide Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:GST-MONOMER.
    ECOL316407:JW1627-MONOMER.
    MetaCyc:GST-MONOMER.
    BRENDAi2.5.1.18. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase GstA (EC:2.5.1.181 Publication)
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 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)DescriptionActionsGraphical viewLength
    Mutagenesisi5Y → F: Does not significantly affect the activity. 1 Publication1
    Mutagenesisi10C → A: 8-fold decrease in affinity for GSH, but 5-fold increase in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. 1 Publication1
    Mutagenesisi10C → S: 6-fold decrease in affinity for GSH, and decrease in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. 1 Publication1
    Mutagenesisi106H → A: Decrease in affinity for GSH while nearly no effect on affinity for CDNB, and decrease in GSH transferase activity. 1 Publication1
    Mutagenesisi106H → F: Decrease in affinity for GSH, while nearly no effect on affinity for CDNB and on GSH transferase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001859701 – 201Glutathione S-transferase GstAAdd BLAST201

    Proteomic databases

    EPDiP0A9D2.
    PaxDbiP0A9D2.
    PRIDEiP0A9D2.

    2D gel databases

    SWISS-2DPAGEP0A9D2.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    BioGridi4260258. 21 interactors.
    DIPiDIP-9851N.
    IntActiP0A9D2. 1 interactor.
    STRINGi511145.b1635.

    Structurei

    Secondary structure

    1201
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 5Combined sources4
    Helixi12 – 20Combined sources9
    Beta strandi26 – 31Combined sources6
    Turni32 – 35Combined sources4
    Helixi43 – 45Combined sources3
    Beta strandi54 – 56Combined sources3
    Beta strandi62 – 65Combined sources4
    Helixi66 – 75Combined sources10
    Helixi78 – 80Combined sources3
    Helixi89 – 104Combined sources16
    Helixi106 – 113Combined sources8
    Beta strandi115 – 117Combined sources3
    Helixi119 – 121Combined sources3
    Helixi122 – 139Combined sources18
    Turni140 – 142Combined sources3
    Beta strandi143 – 145Combined sources3
    Beta strandi146 – 150Combined sources5
    Helixi153 – 167Combined sources15
    Helixi176 – 186Combined sources11
    Helixi189 – 197Combined sources9

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0A9D2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini1 – 81GST N-terminalAdd BLAST81
    Domaini87 – 201GST C-terminalAdd BLAST115

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni65 – 66Glutathione binding1 Publication2
    Regioni103 – 106Glutathione binding1 Publication4

    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

    eggNOGiENOG4108K3A. Bacteria.
    COG0625. LUCA.
    HOGENOMiHOG000125748.
    InParanoidiP0A9D2.
    KOiK00799.
    OMAiSHKLQDG.
    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.
    PF13409. GST_N_2. 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)DescriptionActionsGraphical viewLength
    Sequence conflicti2K → L AA sequence (PubMed:2185038).Curated1
    Sequence conflicti5 – 6YK → IL AA sequence (PubMed:2185038).Curated2

    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_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74707; AAC74707; b1635.
    BAA15396; BAA15396; BAA15396.
    GeneIDi945758.
    KEGGiecj:JW1627.
    eco: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_LN832404.1.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi4260258. 21 interactors.
    DIPiDIP-9851N.
    IntActiP0A9D2. 1 interactor.
    STRINGi511145.b1635.

    2D gel databases

    SWISS-2DPAGEP0A9D2.

    Proteomic databases

    EPDiP0A9D2.
    PaxDbiP0A9D2.
    PRIDEiP0A9D2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74707; AAC74707; b1635.
    BAA15396; BAA15396; BAA15396.
    GeneIDi945758.
    KEGGiecj:JW1627.
    eco:b1635.
    PATRICi32118572. VBIEscCol129921_1706.

    Organism-specific databases

    EchoBASEiEB2497.
    EcoGeneiEG12613. gstA.

    Phylogenomic databases

    eggNOGiENOG4108K3A. Bacteria.
    COG0625. LUCA.
    HOGENOMiHOG000125748.
    InParanoidiP0A9D2.
    KOiK00799.
    OMAiSHKLQDG.
    PhylomeDBiP0A9D2.

    Enzyme and pathway databases

    BioCyciEcoCyc:GST-MONOMER.
    ECOL316407:JW1627-MONOMER.
    MetaCyc:GST-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.
    PF13409. GST_N_2. 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...

    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: November 2, 2016
    This is version 91 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

    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 one 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.