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P0A9D2 (GSTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase GstA

EC=2.5.1.18
Alternative name(s):
GST B1-1
Gene names
Name:gstA
Synonyms:gst
Ordered Locus Names:b1635, JW1627
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.5 Ref.6 Ref.7

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.1 Ref.5 Ref.7

Subunit structure

Homodimer. Ref.1 Ref.5 Ref.8 Ref.9

Subcellular location

Cytoplasm.

Disruption phenotype

Deletion of the gstA gene decreases the resistance of the bacteria to hydrogen peroxide. Ref.6

Sequence similarities

Belongs to the GST superfamily. Beta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

kcat is 9 sec(-1) for the GSH transferase reaction with CDNB as substrate (Ref.7).

KM=0.041 mM for glutathione (Ref.1) Ref.1 Ref.5 Ref.7

KM=0.3 mM for glutathione (Ref.7)

KM=0.99 mM for 1-chloro-2,4-dinitrobenzene (Ref.1)

KM=1.9 mM for 1-chloro-2,4-dinitrobenzene (Ref.7)

pH dependence:

Optimum pH is 7.5 (Ref.1).

Temperature dependence:

Optimum temperature is 35 degrees Celsius (Ref.1).

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processxenobiotic catabolic process

Traceable author statement PubMed 19016852. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from direct assay Ref.1. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Glutathione S-transferase GstA
PRO_0000185970

Regions

Domain1 – 8181GST N-terminal
Domain87 – 201115GST C-terminal
Region65 – 662Glutathione binding
Region103 – 1064Glutathione binding

Sites

Binding site101Glutathione
Binding site351Glutathione
Binding site521Glutathione; via amide nitrogen and carbonyl oxygen
Binding site991Glutathione

Experimental info

Mutagenesis51Y → F: Does not significantly affect the activity. Ref.1
Mutagenesis101C → A: 8-fold decrease in affinity for GSH, but 5-fold increase in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. Ref.7
Mutagenesis101C → S: 6-fold decrease in affinity for GSH, and decrease in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. Ref.7
Mutagenesis1061H → A: Decrease in affinity for GSH while nearly no effect on affinity for CDNB, and decrease in GSH transferase activity. Ref.7
Mutagenesis1061H → F: Decrease in affinity for GSH, while nearly no effect on affinity for CDNB and on GSH transferase activity. Ref.7
Sequence conflict21K → L AA sequence Ref.5
Sequence conflict5 – 62YK → IL AA sequence Ref.5

Secondary structure

................................... 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9D2 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 6347401123B044E2

FASTA20122,868
        10         20         30         40         50         60 
MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DDYFAVNPKG QVPALLLDDG 

        70         80         90        100        110        120 
TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY IATELHKGFT PLFRPDTPEE 

       130        140        150        160        170        180 
YKPTVRAQLE KKLQYVNEAL KDEHWICGQR FTIADAYLFT VLRWAYAVKL NLEGLEHIAA 

       190        200 
FMQRMAERPE VQDALSAEGL K 

« Hide

References

« Hide 'large scale' references
[1]"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."
Nishida M., Kong K.-H., Inoue H., Takahashi K.
J. Biol. Chem. 269:32536-32541(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF TYR-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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."
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. expand/collapse author list , 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.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Purification and study of a bacterial glutathione S-transferase."
Arca P., Garcia P., Hardisson C., Suarez J.E.
FEBS Lett. 263:77-79(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: K12.
[6]"Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress."
Kanai T., Takahashi K., Inoue H.
J. Biochem. 140:703-711(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, DISRUPTION PHENOTYPE.
Strain: K12.
[7]"Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys(10) and His(106)."
Wang X.Y., Zhang Z.R., Perrett S.
Biochem. J. 417:55-64(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-10 AND HIS-106.
[8]"Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106."
Nishida M., Harada S., Noguchi S., Satow Y., Inoue H., Takahashi K.
J. Mol. Biol. 281:135-147(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE SULFONATE, SUBUNIT.
[9]"Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli."
Rife C.L., Parsons J.F., Xiao G., Gilliland G.L., Armstrong R.N.
Proteins 53:777-782(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE SULFONATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38497 Genomic DNA. Translation: BAA07509.1.
U00096 Genomic DNA. Translation: AAC74707.1.
AP009048 Genomic DNA. Translation: BAA15396.1.
PIRA55495.
RefSeqNP_416152.1. NC_000913.3.
YP_489899.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0FX-ray2.10A/B1-201[»]
1N2AX-ray1.90A/B1-201[»]
ProteinModelPortalP0A9D2.
SMRP0A9D2. Positions 1-201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9851N.
IntActP0A9D2. 1 interaction.
STRING511145.b1635.

2D gel databases

SWISS-2DPAGEP0A9D2.

Proteomic databases

PaxDbP0A9D2.
PRIDEP0A9D2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74707; AAC74707; b1635.
BAA15396; BAA15396; BAA15396.
GeneID12931264.
945758.
KEGGecj:Y75_p1612.
eco:b1635.
PATRIC32118572. VBIEscCol129921_1706.

Organism-specific databases

EchoBASEEB2497.
EcoGeneEG12613. gstA.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125748.
KOK00799.
OMAEIHKGFS.
OrthoDBEOG6H1Q01.
PhylomeDBP0A9D2.
ProtClustDBPRK10542.

Enzyme and pathway databases

BioCycEcoCyc:GST-MONOMER.
ECOL316407:JW1627-MONOMER.
MetaCyc:GST-MONOMER.

Gene expression databases

GenevestigatorP0A9D2.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9D2.
PROP0A9D2.

Entry information

Entry nameGSTA_ECOLI
AccessionPrimary (citable) accession number: P0A9D2
Secondary accession number(s): P39100
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene