P46427 (GSTP_ONCVO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase 2
EC=2.5.1.18

Alternative name(s):
GST class-pi

Gene names

Name:

GST2

Organism

Onchocerca volvulus

Taxonomic identifier

6282 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Spirurida › Filarioidea › Onchocercidae › Onchocerca

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Transferase
Technical term	3D-structure
Gene Ontology (GO)
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 208

208

Glutathione S-transferase 2

PRO_0000185914

Regions

Domain

1 – 78

78

GST N-terminal

Domain

80 – 200

121

GST C-terminal

Region

49 – 50

2

Glutathione binding

Region

62 – 63

2

Glutathione binding

Sites

Binding site

7

1

Glutathione

Binding site

42

1

Glutathione By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

208

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Helix

12 – 14

3

Helix

15 – 23

9

Beta strand

29 – 33

5

Helix

35 – 37

3

Turn

39 – 41

3

Helix

42 – 44

3

Beta strand

52 – 55

4

Beta strand

58 – 62

5

Helix

63 – 73

11

Helix

81 – 107

27

Helix

109 – 119

11

Helix

121 – 132

12

Turn

133 – 135

3

Helix

136 – 138

3

Beta strand

139 – 141

3

Beta strand

144 – 146

3

Helix

149 – 164

16

Turn

166 – 171

6

Helix

173 – 183

11

Helix

186 – 197

12

Sequences

	Sequence		Length	Mass (Da)
	P46427 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D3A76450AE7A1321	FASTA	208	24,232
	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

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.

PIR

S41933.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TU7	X-ray	1.50	A/B	1-208	[»]
1TU8	X-ray	1.80	A/B/C/D	1-208	[»]

ProteinModelPortal

P46427.

SMR

P46427. Positions 1-208.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01268. GSTRNSFRASEP.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P46427.

Entry information

Entry name

GSTP_ONCVO

Accession

Primary (citable) accession number: P46427

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)