P30112 (GST26_FASHE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glutathione S-transferase class-mu 26 kDa isozyme 51 Short name=GST51 EC=2.5.1.18 Alternative name(s): Fh51
Organism	Fasciola hepatica (Liver fluke)
Taxonomic identifier	6192 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Platyhelminthes › Trematoda › Digenea › Echinostomida › Echinostomata › Echinostomatoidea › Fasciolidae › Fasciola

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 218

217

Glutathione S-transferase class-mu 26 kDa isozyme 51

PRO_0000185807

Regions

Domain

2 – 83

82

GST N-terminal

Domain

85 – 203

119

GST C-terminal

Region

7 – 8

2

Glutathione binding By similarity

Region

41 – 45

5

Glutathione binding By similarity

Region

54 – 55

2

Glutathione binding By similarity

Region

67 – 68

2

Glutathione binding By similarity

Sites

Binding site

111

1

Substrate By similarity

Experimental info

Sequence conflict

84

1

T → S Ref.3

Sequence conflict

135

1

N → D Ref.3

Sequence conflict

147

1

P → T Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

218

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Turn

12 – 14

3

Helix

15 – 24

10

Beta strand

29 – 33

5

Helix

38 – 44

7

Beta strand

55 – 60

6

Beta strand

63 – 67

5

Helix

68 – 78

11

Helix

86 – 110

25

Helix

115 – 137

23

Beta strand

145 – 147

3

Helix

150 – 162

13

Turn

163 – 165

3

Turn

167 – 172

6

Helix

174 – 184

11

Helix

187 – 194

8

Beta strand

208 – 211

4

Sequences

	Sequence		Length	Mass (Da)
	P30112 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DF8A826E056A2196	FASTA	218	25,373
	10 20 30 40 50 60 MPAKLGYWKI RGLQQPVRLL LEYLGEEYEE HLYGRDDREK WFGDKFNMGL DLPNLPYYID 70 80 90 100 110 120 DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM DLRMGFVRVC YNPKFEEVKG 130 140 150 160 170 180 DYLKELPTTL KMWSNFLGDR HYLTGSPVSH VDFMVYEALD CIRYLAPQCL EDFPKLKEFK 190 200 210 SRIEDLPKIK AYMESEKFIK WPLNSWIASF GGGDAAPA

References

[1]	"Molecular characterization of cDNA sequences encoding glutathione S-transferases of Fasciola hepatica." Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W. Exp. Parasitol. 74:232-237(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Erratum Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W. Exp. Parasitol. 77:385-385(1993) [PubMed] [Europe PMC] [Abstract]
[3]	"Sequence analysis of a Fasciola hepatica glutathione S-transferase cDNA clone." Muro A., Rodriguez-Medina J.R., Hillyer G.V. Am. J. Trop. Med. Hyg. 48:457-463(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-218.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M77682 mRNA. Translation: AAA29141.1.

PIR

A48388.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WRT	X-ray	2.40	A/B/C/D/E/F/G/H/I/J/K/L	1-218	[»]

ProteinModelPortal

P30112.

SMR

P30112. Positions 2-215.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

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

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

P30112.

Entry information

Entry name

GST26_FASHE

Accession

Primary (citable) accession number: P30112

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)