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P46427 (GSTP_ONCVO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

EC=2.5.1.18
Alternative name(s):
GST class-pi
Gene names
Name:GST2
OrganismOnchocerca volvulus
Taxonomic identifier6282 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeOnchocerca

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to play a central role in the parasite detoxification system.

Catalytic activity

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

Subunit structure

Homodimer. Ref.3

Tissue specificity

Hypodermis, wall of the seminal receptacle and spermatozoa of adult worms.

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Gene Ontology (GO)
   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 – 208208Glutathione S-transferase 2
PRO_0000185914

Regions

Domain1 – 7878GST N-terminal
Domain80 – 200121GST C-terminal
Region49 – 502Glutathione binding
Region62 – 632Glutathione binding

Sites

Binding site71Glutathione
Binding site421Glutathione By similarity

Secondary structure

.................................... 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46427 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D3A76450AE7A1321

FASTA20824,232
        10         20         30         40         50         60 
MSYKLTYFSI RGLAEPIRLF LVDQDIKFID DRIAKDDFSS IKSQFQFGQL PCLYDGDQQI 

        70         80         90        100        110        120 
VQSGAILRHL ARKYNLNGEN EMETTYIDMF CEGVRDLHVK YTRMIYMAYE TEKDPYIKSI 

       130        140        150        160        170        180 
LPGELAKFEK LLATRGNGRN LILGDKISYA DYALFEELDV HQILDPHCLD KFPLLKAFHQ 

       190        200 
RMKDRPKLKE YCEKRDAAKV PVNGNGKQ 

« Hide

References

[1]"Molecular characterisation and localisation of an Onchocerca volvulus pi-class glutathione S-transferase."
Salinas G., Braun G., Taylor D.W.
Mol. Biochem. Parasitol. 66:1-9(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Guatemala.
[2]"Onchocerca volvulus: isolation and sequence of a second glutathione S-transferase cDNA."
Liebau E., Walter R.D., Henkle-Duehrsen K.
Exp. Parasitol. 79:68-71(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus."
Perbandt M., Hoppner J., Betzel C., Walter R.D., Liebau E.
J. Biol. Chem. 280:12630-12636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L28771 mRNA. Translation: AAA53575.1.
X77393 mRNA. Translation: CAA54568.1.
PIRS41933.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU7X-ray1.50A/B1-208[»]
1TU8X-ray1.80A/B/C/D1-208[»]
ProteinModelPortalP46427.
SMRP46427. Positions 1-208.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01268. GSTRNSFRASEP.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46427.

Entry information

Entry nameGSTP_ONCVO
AccessionPrimary (citable) accession number: P46427
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references