ID   GSTA_ECOLI              Reviewed;         201 AA.
AC   P0A9D2; P39100;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Glutathione S-transferase GstA;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:7798255};
DE   AltName: Full=GST B1-1;
GN   Name=gstA; Synonyms=gst; OrderedLocusNames=b1635, JW1627;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS
RP   OF TYR-5.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=7798255; DOI=10.1016/s0021-9258(18)31667-3;
RA   Nishida M., Kong K.-H., Inoue H., Takahashi K.;
RT   "Molecular cloning and site-directed mutagenesis of glutathione S-
RT   transferase from Escherichia coli. The conserved tyrosyl residue near the
RT   N-terminus is not essential for catalysis.";
RL   J. Biol. Chem. 269:32536-32541(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=2185038; DOI=10.1016/0014-5793(90)80709-r;
RA   Arca P., Garcia P., Hardisson C., Suarez J.E.;
RT   "Purification and study of a bacterial glutathione S-transferase.";
RL   FEBS Lett. 263:77-79(1990).
RN   [6]
RP   FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=17018556; DOI=10.1093/jb/mvj199;
RA   Kanai T., Takahashi K., Inoue H.;
RT   "Three distinct-type glutathione S-transferases from Escherichia coli
RT   important for defense against oxidative stress.";
RL   J. Biochem. 140:703-711(2006).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND MUTAGENESIS OF CYS-10
RP   AND HIS-106.
RX   PubMed=18778244; DOI=10.1042/bj20071702;
RA   Wang X.Y., Zhang Z.R., Perrett S.;
RT   "Characterization of the activity and folding of the glutathione
RT   transferase from Escherichia coli and the roles of residues Cys(10) and
RT   His(106).";
RL   Biochem. J. 417:55-64(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
RP   SULFONATE, AND SUBUNIT.
RX   PubMed=9680481; DOI=10.1006/jmbi.1998.1927;
RA   Nishida M., Harada S., Noguchi S., Satow Y., Inoue H., Takahashi K.;
RT   "Three-dimensional structure of Escherichia coli glutathione S-transferase
RT   complexed with glutathione sulfonate: catalytic roles of Cys10 and
RT   His106.";
RL   J. Mol. Biol. 281:135-147(1998).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
RP   SULFONATE, AND SUBUNIT.
RX   PubMed=14635120; DOI=10.1002/prot.10452;
RA   Rife C.L., Parsons J.F., Xiao G., Gilliland G.L., Armstrong R.N.;
RT   "Conserved structural elements in glutathione transferase homologues
RT   encoded in the genome of Escherichia coli.";
RL   Proteins 53:777-782(2003).
CC   -!- FUNCTION: Catalyzes the conjugation of reduced glutathione (GSH) to a
CC       wide number of exogenous and endogenous hydrophobic electrophiles.
CC       Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic
CC       acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH
CC       to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of
CC       glutathione-dependent peroxidase activity toward cumene hydroperoxide.
CC       Is important for defense against oxidative stress, probably via its
CC       peroxidase activity. {ECO:0000269|PubMed:17018556,
CC       ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
CC       ECO:0000269|PubMed:7798255}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
CC         ECO:0000269|PubMed:7798255};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.041 mM for glutathione {ECO:0000269|PubMed:18778244,
CC         ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255};
CC         KM=0.3 mM for glutathione {ECO:0000269|PubMed:18778244,
CC         ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255};
CC         KM=0.99 mM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
CC         ECO:0000269|PubMed:7798255};
CC         KM=1.9 mM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
CC         ECO:0000269|PubMed:7798255};
CC         Note=kcat is 9 sec(-1) for the GSH transferase reaction with CDNB as
CC         substrate. {ECO:0000269|PubMed:18778244};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:2185038,
CC         ECO:0000269|PubMed:7798255};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14635120,
CC       ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255,
CC       ECO:0000269|PubMed:9680481}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gstA gene decreases the
CC       resistance of the bacteria to hydrogen peroxide.
CC       {ECO:0000269|PubMed:17018556}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Beta family. {ECO:0000305}.
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DR   EMBL; D38497; BAA07509.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74707.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15396.1; -; Genomic_DNA.
DR   PIR; A55495; A55495.
DR   RefSeq; NP_416152.1; NC_000913.3.
DR   RefSeq; WP_000765749.1; NZ_LN832404.1.
DR   PDB; 1A0F; X-ray; 2.10 A; A/B=1-201.
DR   PDB; 1N2A; X-ray; 1.90 A; A/B=1-201.
DR   PDBsum; 1A0F; -.
DR   PDBsum; 1N2A; -.
DR   AlphaFoldDB; P0A9D2; -.
DR   SMR; P0A9D2; -.
DR   BioGRID; 4260258; 34.
DR   DIP; DIP-9851N; -.
DR   IntAct; P0A9D2; 1.
DR   STRING; 511145.b1635; -.
DR   DrugBank; DB03003; Glutathione sulfonic acid.
DR   jPOST; P0A9D2; -.
DR   PaxDb; 511145-b1635; -.
DR   EnsemblBacteria; AAC74707; AAC74707; b1635.
DR   GeneID; 75204480; -.
DR   GeneID; 945758; -.
DR   KEGG; ecj:JW1627; -.
DR   KEGG; eco:b1635; -.
DR   PATRIC; fig|1411691.4.peg.625; -.
DR   EchoBASE; EB2497; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_1_6; -.
DR   InParanoid; P0A9D2; -.
DR   OMA; LEWLNYV; -.
DR   OrthoDB; 8772754at2; -.
DR   PhylomeDB; P0A9D2; -.
DR   BioCyc; EcoCyc:GST-MONOMER; -.
DR   BioCyc; MetaCyc:GST-MONOMER; -.
DR   BRENDA; 2.5.1.18; 2026.
DR   EvolutionaryTrace; P0A9D2; -.
DR   PRO; PR:P0A9D2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
DR   CDD; cd03188; GST_C_Beta; 1.
DR   CDD; cd03057; GST_N_Beta; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR44051:SF10; GLUTATHIONE S-TRANSFERASE GSTA; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   SWISS-2DPAGE; P0A9D2; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW   Transferase.
FT   CHAIN           1..201
FT                   /note="Glutathione S-transferase GstA"
FT                   /id="PRO_0000185970"
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT   DOMAIN          87..201
FT                   /note="GST C-terminal"
FT   BINDING         10
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:9680481"
FT   BINDING         35
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:9680481"
FT   BINDING         52
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:9680481"
FT   BINDING         65..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:9680481"
FT   BINDING         99
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:9680481"
FT   BINDING         103..106
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:9680481"
FT   MUTAGEN         5
FT                   /note="Y->F: Does not significantly affect the activity."
FT                   /evidence="ECO:0000269|PubMed:7798255"
FT   MUTAGEN         10
FT                   /note="C->A: 8-fold decrease in affinity for GSH, but
FT                   5-fold increase in GSH transferase activity. Loss of
FT                   thiol:disulfide oxidoreductase activity."
FT                   /evidence="ECO:0000269|PubMed:18778244"
FT   MUTAGEN         10
FT                   /note="C->S: 6-fold decrease in affinity for GSH, and
FT                   decrease in GSH transferase activity. Loss of
FT                   thiol:disulfide oxidoreductase activity."
FT                   /evidence="ECO:0000269|PubMed:18778244"
FT   MUTAGEN         106
FT                   /note="H->A: Decrease in affinity for GSH while nearly no
FT                   effect on affinity for CDNB, and decrease in GSH
FT                   transferase activity."
FT                   /evidence="ECO:0000269|PubMed:18778244"
FT   MUTAGEN         106
FT                   /note="H->F: Decrease in affinity for GSH, while nearly no
FT                   effect on affinity for CDNB and on GSH transferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:18778244"
FT   CONFLICT        2
FT                   /note="K -> L (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        5..6
FT                   /note="YK -> IL (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           12..20
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   TURN            32..35
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           66..75
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           89..104
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           122..139
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:1A0F"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           153..167
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:1N2A"
FT   HELIX           189..197
FT                   /evidence="ECO:0007829|PDB:1N2A"
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
//