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P0A9D3

- GSTA_ECO57

UniProt

P0A9D3 - GSTA_ECO57

Protein

Glutathione S-transferase GstA

Gene

gstA

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101GlutathioneBy similarity
    Binding sitei35 – 351GlutathioneBy similarity
    Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei106 – 1061GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-2315-MONOMER.
    ECOO157:GST-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase GstA (EC:2.5.1.18)
    Gene namesi
    Name:gstA
    Synonyms:gst
    Ordered Locus Names:Z2647, ECs2344
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Glutathione S-transferase GstAPRO_0000185971Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi155864.Z2647.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A9D3.
    SMRiP0A9D3. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    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 bindingBy similarity

    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.
    KOiK00799.
    OMAiNYVATEL.
    OrthoDBiEOG6H1Q01.

    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.

    P0A9D3-1 [UniParc]FASTAAdd to Basket

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    MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DDYFAVNPKG    50
    QVPALLLDDG TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY 100
    IATELHKGFT PLFRPDTPEE YKPTVRAQLE KKLQYVNEAL KDEHWICGQR 150
    FTIADAYLFT VLRWAYAVKL NLEGLEHIAA FMQRMAERPE VQDALSAEGL 200
    K 201
    Length:201
    Mass (Da):22,868
    Last modified:July 19, 2005 - v1
    Checksum:i6347401123B044E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56624.1.
    BA000007 Genomic DNA. Translation: BAB35767.1.
    PIRiD85770.
    H90921.
    RefSeqiNP_288071.1. NC_002655.2.
    NP_310371.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG56624; AAG56624; Z2647.
    BAB35767; BAB35767; BAB35767.
    GeneIDi914142.
    961588.
    KEGGiece:Z2647.
    ecs:ECs2344.
    PATRICi18354016. VBIEscCol44059_2221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56624.1 .
    BA000007 Genomic DNA. Translation: BAB35767.1 .
    PIRi D85770.
    H90921.
    RefSeqi NP_288071.1. NC_002655.2.
    NP_310371.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P0A9D3.
    SMRi P0A9D3. Positions 1-201.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z2647.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG56624 ; AAG56624 ; Z2647 .
    BAB35767 ; BAB35767 ; BAB35767 .
    GeneIDi 914142.
    961588.
    KEGGi ece:Z2647.
    ecs:ECs2344.
    PATRICi 18354016. VBIEscCol44059_2221.

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000125748.
    KOi K00799.
    OMAi NYVATEL.
    OrthoDBi EOG6H1Q01.

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-2315-MONOMER.
    ECOO157:GST-MONOMER.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiGSTA_ECO57
    AccessioniPrimary (citable) accession number: P0A9D3
    Secondary accession number(s): P39100
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 61 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

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3