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P0A9D3 (GSTA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Gene names
Name:gstA
Synonyms:gst
Ordered Locus Names:Z2647, ECs2344
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles By similarity.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the GST superfamily. Beta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Glutathione S-transferase GstA
PRO_0000185971

Regions

Domain1 – 8181GST N-terminal
Domain87 – 201115GST C-terminal
Region65 – 662Glutathione binding By similarity

Sites

Binding site101Glutathione By similarity
Binding site351Glutathione By similarity
Binding site521Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Binding site1061Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9D3 [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

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56624.1.
BA000007 Genomic DNA. Translation: BAB35767.1.
PIRD85770.
H90921.
RefSeqNP_288071.1. NC_002655.2.
NP_310371.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A9D3.
SMRP0A9D3. Positions 1-201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z2647.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56624; AAG56624; Z2647.
BAB35767; BAB35767; BAB35767.
GeneID914142.
961588.
KEGGece:Z2647.
ecs:ECs2344.
PATRIC18354016. VBIEscCol44059_2221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECOL386585:GJFA-2315-MONOMER.
ECOO157:GST-MONOMER.

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...

Entry information

Entry nameGSTA_ECO57
AccessionPrimary (citable) accession number: P0A9D3
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 59 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