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P30112 (GST26_FASHE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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 51

Short name=GST51
EC=2.5.1.18
Alternative name(s):
Fh51
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.

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 By similarity
Chain2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme 51
PRO_0000185807

Regions

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

Sites

Binding site1111Substrate By similarity

Experimental info

Sequence conflict841T → S Ref.3
Sequence conflict1351N → D Ref.3
Sequence conflict1471P → T Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30112 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DF8A826E056A2196

FASTA21825,373
        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 

« 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]"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.
PIRA48388.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WRTX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-218[»]
ProteinModelPortalP30112.
SMRP30112. 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

EvolutionaryTraceP30112.

Entry information

Entry nameGST26_FASHE
AccessionPrimary (citable) accession number: P30112
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 72 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