Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A9D2

- GSTA_ECOLI

UniProt

P0A9D2 - GSTA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutathione S-transferase GstA

Gene

gstA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.3 Publications

Kineticsi

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

  1. KM=0.041 mM for glutathione3 Publications
  2. KM=0.3 mM for glutathione3 Publications
  3. KM=0.99 mM for 1-chloro-2,4-dinitrobenzene3 Publications
  4. KM=1.9 mM for 1-chloro-2,4-dinitrobenzene3 Publications

pH dependencei

Optimum pH is 7.5.2 Publications

Temperature dependencei

Optimum temperature is 35 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione
Binding sitei35 – 351Glutathione
Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen
Binding sitei99 – 991Glutathione

GO - Molecular functioni

  1. glutathione transferase activity Source: EcoCyc

GO - Biological processi

  1. xenobiotic catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:GST-MONOMER.
ECOL316407:JW1627-MONOMER.
MetaCyc:GST-MONOMER.
RETL1328306-WGS:GSTH-1203-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase GstA (EC:2.5.1.18)
Alternative name(s):
GST B1-1
Gene namesi
Name:gstA
Synonyms:gst
Ordered Locus Names:b1635, JW1627
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12613. gstA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Deletion of the gstA gene decreases the resistance of the bacteria to hydrogen peroxide.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51Y → F: Does not significantly affect the activity. 1 Publication
Mutagenesisi10 – 101C → A: 8-fold decrease in affinity for GSH, but 5-fold increase in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. 1 Publication
Mutagenesisi10 – 101C → S: 6-fold decrease in affinity for GSH, and decrease in GSH transferase activity. Loss of thiol:disulfide oxidoreductase activity. 1 Publication
Mutagenesisi106 – 1061H → A: Decrease in affinity for GSH while nearly no effect on affinity for CDNB, and decrease in GSH transferase activity. 1 Publication
Mutagenesisi106 – 1061H → F: Decrease in affinity for GSH, while nearly no effect on affinity for CDNB and on GSH transferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Glutathione S-transferase GstAPRO_0000185970Add
BLAST

Proteomic databases

PaxDbiP0A9D2.
PRIDEiP0A9D2.

2D gel databases

SWISS-2DPAGEP0A9D2.

Expressioni

Gene expression databases

GenevestigatoriP0A9D2.

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

DIPiDIP-9851N.
IntActiP0A9D2. 1 interaction.
STRINGi511145.b1635.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54
Helixi12 – 209
Beta strandi26 – 316
Turni32 – 354
Helixi43 – 453
Beta strandi54 – 563
Beta strandi62 – 654
Helixi66 – 7510
Helixi78 – 803
Helixi89 – 10416
Helixi106 – 1138
Beta strandi115 – 1173
Helixi119 – 1213
Helixi122 – 13918
Turni140 – 1423
Beta strandi143 – 1453
Beta strandi146 – 1505
Helixi153 – 16715
Helixi176 – 18611
Helixi189 – 1979

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0FX-ray2.10A/B1-201[»]
1N2AX-ray1.90A/B1-201[»]
ProteinModelPortaliP0A9D2.
SMRiP0A9D2. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9D2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8181GST N-terminalAdd
BLAST
Domaini87 – 201115GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 662Glutathione binding
Regioni103 – 1064Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Beta family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125748.
InParanoidiP0A9D2.
KOiK00799.
OMAiNYVATEL.
OrthoDBiEOG6H1Q01.
PhylomeDBiP0A9D2.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9D2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DDYFAVNPKG
60 70 80 90 100
QVPALLLDDG TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY
110 120 130 140 150
IATELHKGFT PLFRPDTPEE YKPTVRAQLE KKLQYVNEAL KDEHWICGQR
160 170 180 190 200
FTIADAYLFT VLRWAYAVKL NLEGLEHIAA FMQRMAERPE VQDALSAEGL

K
Length:201
Mass (Da):22,868
Last modified:July 19, 2005 - v1
Checksum:i6347401123B044E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21K → L AA sequence (PubMed:2185038)Curated
Sequence conflicti5 – 62YK → IL AA sequence (PubMed:2185038)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38497 Genomic DNA. Translation: BAA07509.1.
U00096 Genomic DNA. Translation: AAC74707.1.
AP009048 Genomic DNA. Translation: BAA15396.1.
PIRiA55495.
RefSeqiNP_416152.1. NC_000913.3.
YP_489899.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74707; AAC74707; b1635.
BAA15396; BAA15396; BAA15396.
GeneIDi12931264.
945758.
KEGGiecj:Y75_p1612.
eco:b1635.
PATRICi32118572. VBIEscCol129921_1706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38497 Genomic DNA. Translation: BAA07509.1 .
U00096 Genomic DNA. Translation: AAC74707.1 .
AP009048 Genomic DNA. Translation: BAA15396.1 .
PIRi A55495.
RefSeqi NP_416152.1. NC_000913.3.
YP_489899.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A0F X-ray 2.10 A/B 1-201 [» ]
1N2A X-ray 1.90 A/B 1-201 [» ]
ProteinModelPortali P0A9D2.
SMRi P0A9D2. Positions 1-201.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9851N.
IntActi P0A9D2. 1 interaction.
STRINGi 511145.b1635.

2D gel databases

SWISS-2DPAGE P0A9D2.

Proteomic databases

PaxDbi P0A9D2.
PRIDEi P0A9D2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74707 ; AAC74707 ; b1635 .
BAA15396 ; BAA15396 ; BAA15396 .
GeneIDi 12931264.
945758.
KEGGi ecj:Y75_p1612.
eco:b1635.
PATRICi 32118572. VBIEscCol129921_1706.

Organism-specific databases

EchoBASEi EB2497.
EcoGenei EG12613. gstA.

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000125748.
InParanoidi P0A9D2.
KOi K00799.
OMAi NYVATEL.
OrthoDBi EOG6H1Q01.
PhylomeDBi P0A9D2.

Enzyme and pathway databases

BioCyci EcoCyc:GST-MONOMER.
ECOL316407:JW1627-MONOMER.
MetaCyc:GST-MONOMER.
RETL1328306-WGS:GSTH-1203-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A9D2.
PROi P0A9D2.

Gene expression databases

Genevestigatori P0A9D2.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiGSTA_ECOLI
AccessioniPrimary (citable) accession number: P0A9D2
Secondary accession number(s): P39100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3