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P31670 (GST27_FASHE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase class-mu 26 kDa isozyme 47

Short name=GST47
EC=2.5.1.18
Alternative name(s):
Fh47
OrganismFasciola hepatica (Liver fluke)
Taxonomic identifier6192 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.4

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 componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme 47
PRO_0000185808

Regions

Domain2 – 8382GST N-terminal
Domain85 – 203119GST C-terminal
Region7 – 82Glutathione binding
Region41 – 455Glutathione binding
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Sites

Binding site1111Substrate By similarity

Experimental info

Sequence conflict661T → I in CAA00121. Ref.3
Sequence conflict103 – 1064RIGF → FEEL Ref.3

Secondary structure

....................................... 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31670 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3FF8B667232663B3

FASTA21825,412
        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 

« Hide

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]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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHEX-ray3.00A2-218[»]
ProteinModelPortalP31670.
SMRP31670. Positions 2-215.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP31670.

Entry information

Entry nameGST27_FASHE
AccessionPrimary (citable) accession number: P31670
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references