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P82999 (GSTE1_PSEUO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione S-transferase

EC=2.5.1.18
OrganismPseudomonas sp. (strain M1)
Taxonomic identifier95619 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.1

Catalytic activity

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

Subunit structure

Monomer and homodimer. Ref.1

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the GST superfamily. UniProtKB P45875

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processmetabolic process

Non-traceable author statement Ref.1. Source: GOC

   Cellular_componentcytoplasm

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionglutathione transferase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›15Glutathione S-transferase
PRO_0000185979

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P82999 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 0E2A0FC5F55CBAC2

FASTA151,817
        10 
MDYLITFYHS PQTNS 

« Hide

References

[1]"Occurrence and properties of glutathione S-transferases in phenol-degrading Pseudomonas strains."
Santos P.M., Mignogna G., Heipieper H.J., Zennaro E.
Res. Microbiol. 153:89-98(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameGSTE1_PSEUO
AccessionPrimary (citable) accession number: P82999
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 23 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