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Reviewed, UniProtKB/Swiss-Prot P30112 (GST26_FASHE)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 transcript 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
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglutathione transferase activity

Inferred from electronic annotation. Source: 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

Sites

Active site71 By similarity

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
P30112-1 [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: 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]"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: 7682383] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-218.

Cross-references

Sequence databases

M77682 mRNA. Translation: AAA29141.1.
PIRA48388.

3D structure databases

HSSPHSSP built from PDB template 1FHE based on UniProtKB P31670.
SMRP30112. Positions 2-215.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.18. 39370.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 56 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents