[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-4894(92)90051-B; PubMed=1740183 [NCBI, ExPASy, EBI, Israel, Japan] Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.; "Molecular characterization of cDNA sequences encoding glutathione S-transferases of Fasciola hepatica."; Exp. Parasitol. 74:232-237(1992).
[2]	ERRATUM. DOI=10.1006/expr.1993.1097; PubMed=8224094 [NCBI, ExPASy, EBI, Israel, Japan] Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.; Exp. Parasitol. 77:385-385(1993).
[3]	NUCLEOTIDE SEQUENCE OF 8-106. Crameri S.; Patent number WO9008819, 09-AUG-1990.
[4]	X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS). DOI=10.1006/jmbi.1997.1338; PubMed=9367777 [NCBI, ExPASy, EBI, Israel, Japan] Rossjohn J., Feil S.C., Wilce M.C.J., Sexton J.L., Spithill T.W., Parker M.W.; "Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase."; J. Mol. Biol. 273:857-872(1997).

Comments

FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
FUNCTION: 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: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the GST superfamily. Mu family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M77681; AAA29140.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A00996; CAA00121.1; -; Unassigned_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1FHE; X-ray; 3.00 A; A=1-218.

[ExPASy / RCSB / EBI]

PDBsum

1FHE; -.

ModBase

P31670.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P31670.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 218`	`217`	`Glutathione S-transferase class-mu 26 kDa isozyme 47.`	`PRO_0000185808`
`DOMAIN`	`2 83`	`82`	`GST N-terminal.`
`DOMAIN`	`85 203`	`119`	`GST C-terminal.`
`ACT_SITE`	`7 7`		`By similarity.`
`CONFLICT`	`66 66`		`T -> I (in Ref. 3; CAA00121).`
`CONFLICT`	`103 106`		`RIGF -> FEEL (in Ref. 3).`
`STRAND`	`4 10`	`7`
`TURN`	`12 14`	`3`
`HELIX`	`15 23`	`9`
`STRAND`	`29 33`	`5`
`HELIX`	`39 42`	`4`
`TURN`	`43 47`	`5`
`STRAND`	`55 59`	`5`
`STRAND`	`64 67`	`4`
`HELIX`	`70 77`	`8`
`TURN`	`78 80`	`3`
`HELIX`	`86 107`	`22`
`STRAND`	`110 112`	`3`
`HELIX`	`115 122`	`8`
`TURN`	`123 125`	`3`
`HELIX`	`126 137`	`12`
`STRAND`	`145 147`	`3`
`HELIX`	`150 162`	`13`
`TURN`	`163 165`	`3`
`HELIX`	`167 170`	`4`
`HELIX`	`174 185`	`12`
`HELIX`	`187 192`	`6`
`STRAND`	`206 211`	`6`

Sequence information

Length: 218 AA [This is the length of the unprocessed precursor]

Molecular weight: 25412 Da [This is the MW of the unprocessed precursor]

CRC64: 3FF8B667232663B3 [This is a checksum on the sequence]

        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

P31670 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools