Reviewed, UniProtKB/Swiss-Prot P31670 (GST27_FASHE)

Names and origin

Protein names	Recommended name:     Glutathione S-transferase class-mu 26 kDa isozyme 47       Short name=GST47     EC=2.5.1.18 Alternative name(s):     Fh47
Organism	Fasciola hepatica (Liver fluke)
Taxonomic identifier	6192 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › 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

Chain

2 – 218

217

Glutathione S-transferase class-mu 26 kDa isozyme 47

PRO_0000185808

Regions

Domain

2 – 83

82

GST N-terminal

Domain

85 – 203

119

GST C-terminal

Sites

Active site

7

1

By similarity

Experimental info

Sequence conflict

66

1

T → I in CAA00121. Ref.3

Sequence conflict

103 – 106

4

RIGF → FEEL Ref.3

Secondary structure

1

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218

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Turn

12 – 14

3

Helix

15 – 23

9

Beta strand

29 – 33

5

Helix

39 – 42

4

Turn

43 – 47

5

Beta strand

55 – 59

5

Beta strand

64 – 67

4

Helix

70 – 77

8

Turn

78 – 80

3

Helix

86 – 107

22

Beta strand

110 – 112

3

Helix

115 – 122

8

Turn

123 – 125

3

Helix

126 – 137

12

Beta strand

145 – 147

3

Helix

150 – 162

13

Turn

163 – 165

3

Helix

167 – 170

4

Helix

174 – 185

12

Helix

187 – 192

6

Beta strand

206 – 211

6

Sequences

	Sequence		Length	Mass (Da)
	P31670-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3FF8B667232663B3	FASTA	218	25,412
	10 20 30 40 50 60 MPAKLGYWKL RGLAQPVRLF LEYLGEEYEE HLYGRDDREK WMSEKFNMGL DLPNLPYYID 70 80 90 100 110 120 DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM DLRIGFGRVC YNPKFEEVKE 130 140 150 160 170 180 EYVKELPKTL KMWSDFLGDR HYLTGSSVSH VDFMLYETLD SIRYLAPHCL DEFPKLKEFK 190 200 210 SRIEALPKIK AYMESKRFIK WPLNGWAASF GAGDAPPS

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: 1740183] [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: 8224094] [Abstract]
[3]	Crameri S. Patent number WO9008819, 09-AUG-1990 Cited for: NUCLEOTIDE SEQUENCE OF 8-106.
[4]	"Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase." Rossjohn J., Feil S.C., Wilce M.C.J., Sexton J.L., Spithill T.W., Parker M.W. J. Mol. Biol. 273:857-872(1997) [PubMed: 9367777] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M77681 mRNA. Translation: AAA29140.1.
A00996 Unassigned RNA. Translation: CAA00121.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FHE	X-ray	3.00	A	2-218	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.5.1.18. 39370.

Family and domain databases

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.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

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

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

GST27_FASHE

Accession

Primary (citable) accession number: P31670

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)