Skip Header

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

Glutathione S-transferase 2

Gene

GST2

Organism
Onchocerca volvulus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Glutathione
Binding sitei42 – 421GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 4401.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 2 (EC:2.5.1.18)
Alternative name(s):
GST class-pi
Gene namesi
Name:GST2
OrganismiOnchocerca volvulus
Taxonomic identifieri6282 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeOnchocerca
ProteomesiUP000024404 Componenti: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208Glutathione S-transferase 2PRO_0000185914Add
BLAST

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi29 – 335Combined sources
Helixi35 – 373Combined sources
Turni39 – 413Combined sources
Helixi42 – 443Combined sources
Beta strandi52 – 554Combined sources
Beta strandi58 – 625Combined sources
Helixi63 – 7311Combined sources
Helixi81 – 10727Combined sources
Helixi109 – 11911Combined sources
Helixi121 – 13212Combined sources
Turni133 – 1353Combined sources
Helixi136 – 1383Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi144 – 1463Combined sources
Helixi149 – 16416Combined sources
Turni166 – 1716Combined sources
Helixi173 – 18311Combined sources
Helixi186 – 19712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU7X-ray1.50A/B1-208[»]
1TU8X-ray1.80A/B/C/D1-208[»]
ProteinModelPortaliP46427.
SMRiP46427. Positions 1-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46427.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7878GST N-terminalAdd
BLAST
Domaini80 – 200121GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 502Glutathione binding
Regioni62 – 632Glutathione binding

Sequence similaritiesi

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

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYKLTYFSI RGLAEPIRLF LVDQDIKFID DRIAKDDFSS IKSQFQFGQL
60 70 80 90 100
PCLYDGDQQI VQSGAILRHL ARKYNLNGEN EMETTYIDMF CEGVRDLHVK
110 120 130 140 150
YTRMIYMAYE TEKDPYIKSI LPGELAKFEK LLATRGNGRN LILGDKISYA
160 170 180 190 200
DYALFEELDV HQILDPHCLD KFPLLKAFHQ RMKDRPKLKE YCEKRDAAKV

PVNGNGKQ
Length:208
Mass (Da):24,232
Last modified:October 31, 1995 - v1
Checksum:iD3A76450AE7A1321
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28771 mRNA. Translation: AAA53575.1.
X77393 mRNA. Translation: CAA54568.1.
PIRiS41933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28771 mRNA. Translation: AAA53575.1.
X77393 mRNA. Translation: CAA54568.1.
PIRiS41933.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU7X-ray1.50A/B1-208[»]
1TU8X-ray1.80A/B/C/D1-208[»]
ProteinModelPortaliP46427.
SMRiP46427. Positions 1-208.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.5.1.18. 4401.

Miscellaneous databases

EvolutionaryTraceiP46427.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1993) [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(1993) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE, SUBUNIT.

Entry informationi

Entry nameiGSTP_ONCVO
AccessioniPrimary (citable) accession number: P46427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: March 31, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.