GSTA_ECOLI
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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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 SWISS-2DPAGE; P0A9D2; -.
DR jPOST; P0A9D2; -.
DR PaxDb; P0A9D2; -.
DR PRIDE; P0A9D2; -.
DR EnsemblBacteria; AAC74707; AAC74707; b1635.
DR EnsemblBacteria; BAA15396; BAA15396; BAA15396.
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; YVATELH; -.
DR PhylomeDB; P0A9D2; -.
DR BioCyc; EcoCyc:GST-MON; -.
DR BioCyc; MetaCyc:GST-MON; -.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
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; PF02798; GST_N; 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 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 5-
FT 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
