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Glutathione S-transferase GstA (EC 2.5.1.18) (GST B1-1)

 GSTA_ECOLI              Reviewed;         201 AA.
P0A9D2; P39100;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
25-OCT-2017, entry version 98.
RecName: Full=Glutathione S-transferase GstA;
EC=2.5.1.18 {ECO:0000269|PubMed:7798255};
AltName: Full=GST B1-1;
Name=gstA; Synonyms=gst; OrderedLocusNames=b1635, JW1627;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
MUTAGENESIS OF TYR-5.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7798255;
Nishida M., Kong K.-H., Inoue H., Takahashi K.;
"Molecular cloning and site-directed mutagenesis of glutathione S-
transferase from Escherichia coli. The conserved tyrosyl residue near
the N-terminus is not essential for catalysis.";
J. Biol. Chem. 269:32536-32541(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=K12;
PubMed=2185038; DOI=10.1016/0014-5793(90)80709-R;
Arca P., Garcia P., Hardisson C., Suarez J.E.;
"Purification and study of a bacterial glutathione S-transferase.";
FEBS Lett. 263:77-79(1990).
[6]
FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, AND DISRUPTION
PHENOTYPE.
STRAIN=K12;
PubMed=17018556; DOI=10.1093/jb/mvj199;
Kanai T., Takahashi K., Inoue H.;
"Three distinct-type glutathione S-transferases from Escherichia coli
important for defense against oxidative stress.";
J. Biochem. 140:703-711(2006).
[7]
FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND MUTAGENESIS OF
CYS-10 AND HIS-106.
PubMed=18778244; DOI=10.1042/BJ20071702;
Wang X.Y., Zhang Z.R., Perrett S.;
"Characterization of the activity and folding of the glutathione
transferase from Escherichia coli and the roles of residues Cys(10)
and His(106).";
Biochem. J. 417:55-64(2009).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
SULFONATE, AND SUBUNIT.
PubMed=9680481; DOI=10.1006/jmbi.1998.1927;
Nishida M., Harada S., Noguchi S., Satow Y., Inoue H., Takahashi K.;
"Three-dimensional structure of Escherichia coli glutathione S-
transferase complexed with glutathione sulfonate: catalytic roles of
Cys10 and His106.";
J. Mol. Biol. 281:135-147(1998).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
SULFONATE, AND SUBUNIT.
PubMed=14635120; DOI=10.1002/prot.10452;
Rife C.L., Parsons J.F., Xiao G., Gilliland G.L., Armstrong R.N.;
"Conserved structural elements in glutathione transferase homologues
encoded in the genome of Escherichia coli.";
Proteins 53:777-782(2003).
-!- FUNCTION: 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. {ECO:0000269|PubMed:17018556,
ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
ECO:0000269|PubMed:7798255}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
ECO:0000269|PubMed:7798255}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.041 mM for glutathione {ECO:0000269|PubMed:18778244,
ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255};
KM=0.3 mM for glutathione {ECO:0000269|PubMed:18778244,
ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255};
KM=0.99 mM for 1-chloro-2,4-dinitrobenzene
{ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
ECO:0000269|PubMed:7798255};
KM=1.9 mM for 1-chloro-2,4-dinitrobenzene
{ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038,
ECO:0000269|PubMed:7798255};
Note=kcat is 9 sec(-1) for the GSH transferase reaction with
CDNB as substrate. {ECO:0000269|PubMed:18778244};
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:2185038,
ECO:0000269|PubMed:7798255};
Temperature dependence:
Optimum temperature is 35 degrees Celsius.
{ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14635120,
ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255,
ECO:0000269|PubMed:9680481}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DISRUPTION PHENOTYPE: Deletion of the gstA gene decreases the
resistance of the bacteria to hydrogen peroxide.
{ECO:0000269|PubMed:17018556}.
-!- SIMILARITY: Belongs to the GST superfamily. Beta family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D38497; BAA07509.1; -; Genomic_DNA.
EMBL; U00096; AAC74707.1; -; Genomic_DNA.
EMBL; AP009048; BAA15396.1; -; Genomic_DNA.
PIR; A55495; A55495.
RefSeq; NP_416152.1; NC_000913.3.
RefSeq; WP_000765749.1; NZ_LN832404.1.
PDB; 1A0F; X-ray; 2.10 A; A/B=1-201.
PDB; 1N2A; X-ray; 1.90 A; A/B=1-201.
PDBsum; 1A0F; -.
PDBsum; 1N2A; -.
ProteinModelPortal; P0A9D2; -.
SMR; P0A9D2; -.
BioGrid; 4260258; 21.
DIP; DIP-9851N; -.
IntAct; P0A9D2; 1.
STRING; 316385.ECDH10B_1769; -.
DrugBank; DB03003; Glutathione Sulfonic Acid.
SWISS-2DPAGE; P0A9D2; -.
PaxDb; P0A9D2; -.
PRIDE; P0A9D2; -.
EnsemblBacteria; AAC74707; AAC74707; b1635.
EnsemblBacteria; BAA15396; BAA15396; BAA15396.
GeneID; 945758; -.
KEGG; ecj:JW1627; -.
KEGG; eco:b1635; -.
PATRIC; fig|1411691.4.peg.625; -.
EchoBASE; EB2497; -.
EcoGene; EG12613; gstA.
eggNOG; ENOG4108K3A; Bacteria.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125748; -.
InParanoid; P0A9D2; -.
KO; K00799; -.
PhylomeDB; P0A9D2; -.
BioCyc; EcoCyc:GST-MONOMER; -.
BioCyc; MetaCyc:GST-MONOMER; -.
BRENDA; 2.5.1.18; 2026.
EvolutionaryTrace; P0A9D2; -.
PRO; PR:P0A9D2; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004364; F:glutathione transferase activity; IDA:EcoCyc.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF13409; GST_N_2; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Reference proteome; Transferase.
CHAIN 1 201 Glutathione S-transferase GstA.
/FTId=PRO_0000185970.
DOMAIN 1 81 GST N-terminal.
DOMAIN 87 201 GST C-terminal.
REGION 65 66 Glutathione binding.
{ECO:0000305|PubMed:9680481}.
REGION 103 106 Glutathione binding.
{ECO:0000305|PubMed:9680481}.
BINDING 10 10 Glutathione.
{ECO:0000305|PubMed:9680481}.
BINDING 35 35 Glutathione.
{ECO:0000305|PubMed:9680481}.
BINDING 52 52 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000305|PubMed:9680481}.
BINDING 99 99 Glutathione.
{ECO:0000305|PubMed:9680481}.
MUTAGEN 5 5 Y->F: Does not significantly affect the
activity. {ECO:0000269|PubMed:7798255}.
MUTAGEN 10 10 C->A: 8-fold decrease in affinity for
GSH, but 5-fold increase in GSH
transferase activity. Loss of
thiol:disulfide oxidoreductase activity.
{ECO:0000269|PubMed:18778244}.
MUTAGEN 10 10 C->S: 6-fold decrease in affinity for
GSH, and decrease in GSH transferase
activity. Loss of thiol:disulfide
oxidoreductase activity.
{ECO:0000269|PubMed:18778244}.
MUTAGEN 106 106 H->A: Decrease in affinity for GSH while
nearly no effect on affinity for CDNB,
and decrease in GSH transferase activity.
{ECO:0000269|PubMed:18778244}.
MUTAGEN 106 106 H->F: Decrease in affinity for GSH, while
nearly no effect on affinity for CDNB and
on GSH transferase activity.
{ECO:0000269|PubMed:18778244}.
CONFLICT 2 2 K -> L (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 5 6 YK -> IL (in Ref. 5; AA sequence).
{ECO:0000305}.
STRAND 2 5 {ECO:0000244|PDB:1N2A}.
HELIX 12 20 {ECO:0000244|PDB:1N2A}.
STRAND 26 31 {ECO:0000244|PDB:1N2A}.
TURN 32 35 {ECO:0000244|PDB:1N2A}.
HELIX 43 45 {ECO:0000244|PDB:1N2A}.
STRAND 54 56 {ECO:0000244|PDB:1N2A}.
STRAND 62 65 {ECO:0000244|PDB:1N2A}.
HELIX 66 75 {ECO:0000244|PDB:1N2A}.
HELIX 78 80 {ECO:0000244|PDB:1N2A}.
HELIX 89 104 {ECO:0000244|PDB:1N2A}.
HELIX 106 113 {ECO:0000244|PDB:1N2A}.
STRAND 115 117 {ECO:0000244|PDB:1N2A}.
HELIX 119 121 {ECO:0000244|PDB:1N2A}.
HELIX 122 139 {ECO:0000244|PDB:1N2A}.
TURN 140 142 {ECO:0000244|PDB:1N2A}.
STRAND 143 145 {ECO:0000244|PDB:1A0F}.
STRAND 146 150 {ECO:0000244|PDB:1N2A}.
HELIX 153 167 {ECO:0000244|PDB:1N2A}.
HELIX 176 186 {ECO:0000244|PDB:1N2A}.
HELIX 189 197 {ECO:0000244|PDB:1N2A}.
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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