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Database: UniProt/SWISS-PROT
Entry: GSTA_ECO57
LinkDB: GSTA_ECO57
Original site: GSTA_ECO57 
ID   GSTA_ECO57              Reviewed;         201 AA.
AC   P0A9D3; P39100;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   07-NOV-2018, entry version 83.
DE   RecName: Full=Glutathione S-transferase GstA;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P0A9D2};
GN   Name=gstA; Synonyms=gst; OrderedLocusNames=Z2647, ECs2344;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000250|UniProtKB:P0A9D2}.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC       {ECO:0000250|UniProtKB:P0A9D2}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9D2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Beta family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG56624.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35767.1; -; Genomic_DNA.
DR   PIR; D85770; D85770.
DR   PIR; H90921; H90921.
DR   RefSeq; NP_310371.1; NC_002695.1.
DR   RefSeq; WP_000765749.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; P0A9D3; -.
DR   SMR; P0A9D3; -.
DR   STRING; 155864.Z2647; -.
DR   EnsemblBacteria; AAG56624; AAG56624; Z2647.
DR   EnsemblBacteria; BAB35767; BAB35767; BAB35767.
DR   GeneID; 914142; -.
DR   KEGG; ece:Z2647; -.
DR   KEGG; ecs:ECs2344; -.
DR   PATRIC; fig|386585.9.peg.2453; -.
DR   eggNOG; ENOG4108K3A; Bacteria.
DR   eggNOG; COG0625; LUCA.
DR   HOGENOM; HOG000125748; -.
DR   KO; K00799; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN         1    201       Glutathione S-transferase GstA.
FT                                /FTId=PRO_0000185971.
FT   DOMAIN        1     81       GST N-terminal.
FT   DOMAIN       87    201       GST C-terminal.
FT   REGION       65     66       Glutathione binding.
FT                                {ECO:0000250|UniProtKB:P0A9D2}.
FT   REGION      103    106       Glutathione binding.
FT                                {ECO:0000250|UniProtKB:P0A9D2}.
FT   BINDING      10     10       Glutathione.
FT                                {ECO:0000250|UniProtKB:P0A9D2}.
FT   BINDING      35     35       Glutathione.
FT                                {ECO:0000250|UniProtKB:P0A9D2}.
FT   BINDING      52     52       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0A9D2}.
FT   BINDING      99     99       Glutathione.
FT                                {ECO:0000250|UniProtKB:P0A9D2}.
SQ   SEQUENCE   201 AA;  22868 MW;  6347401123B044E2 CRC64;
     MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DDYFAVNPKG QVPALLLDDG
     TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY IATELHKGFT PLFRPDTPEE
     YKPTVRAQLE KKLQYVNEAL KDEHWICGQR FTIADAYLFT VLRWAYAVKL NLEGLEHIAA
     FMQRMAERPE VQDALSAEGL K
//
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