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P56598 (GST29_FASHE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. 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 1

Short name=GST1
EC=2.5.1.18
Alternative name(s):
Fh1
OrganismFasciola hepatica (Liver fluke)
Taxonomic identifier6192 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

Protein attributes

Sequence length221 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

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Gene Ontology (GO)
   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 By similarity
Chain2 – 221220Glutathione S-transferase class-mu 26 kDa isozyme 1
PRO_0000185810

Regions

Domain2 – 8281GST N-terminal
Domain84 – 202119GST C-terminal
Region7 – 82Glutathione binding
Region40 – 445Glutathione binding
Region53 – 542Glutathione binding
Region66 – 672Glutathione binding

Sites

Binding site1101Substrate By similarity

Experimental info

Sequence conflict231Y → V in CAA00118. Ref.3
Sequence conflict111 – 1122DP → VS in CAA00118. Ref.3
Sequence conflict1901A → P in CAA00118. Ref.3

Secondary structure

................................... 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56598 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 17EAF460F750895F

FASTA22125,730
        10         20         30         40         50         60 
MPAKLGYWKI RGLQQPVRLL LEYGEKYEEQ IYERDDGEKW FSKKFELGLD LPNLPYYIDD 

        70         80         90        100        110        120 
KCKLTQSLAI LRYIADKHGM IGSTPEERAR VSMIEGAAVD LRQGLSRISY DPKFEQLKEG 

       130        140        150        160        170        180 
YLKDLPTTMK MWSDFLGKNP YLRGTSVSHV DFMVYEALDA IRYLEPHCLD HFPNLQQFMS 

       190        200        210        220 
RIEALPSIKA YMESNRFIKW PLNGWHAQFG GGDAPPSHEK K 

« 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 23-221.
[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 (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
A00993 Unassigned RNA. Translation: CAA00118.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FHEX-ray2.30A/B2-216[»]
ProteinModelPortalP56598.
SMRP56598. Positions 2-216.
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.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56598.

Entry information

Entry nameGST29_FASHE
AccessionPrimary (citable) accession number: P56598
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 71 of the entry and version 2 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