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Reviewed, UniProtKB/Swiss-Prot P30113 (GST28_SCHBO)

Last modified November 24, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 28 kDa isozyme
      Short name=GST 28
    EC=2.5.1.18
Alternative name(s):
    Sb28GST
OrganismSchistosoma bovis (Blood fluke)
Taxonomic identifier6184 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
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.

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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Glutathione S-transferase class-mu 28 kDa isozyme
PRO_0000185812

Regions

Domain4 – 8683GST N-terminal
Domain88 – 211124GST C-terminal

Sites

Active site101

Secondary structure

................................. 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30113-1 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 9B9F1358710D3C76

FASTA21123,898
        10         20         30         40         50         60 
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG GRLPAVKITD 

        70         80         90        100        110        120 
NHGHVKWMVE SLAIARYMAK KHHMMGGTEE EYYNVEKLIG QAEDLEHEYY KTLMKPEEEK 

       130        140        150        160        170        180 
QKIIKEILNG KVPVLLDIIC ESLKASTGKL AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG 

       190        200        210 
KYPEIHKHRE NLLASSPRLA KYLSDRAATP F 

« Hide

References

[1]"Inter-species variation of schistosome 28-kDa glutathione S-transferases."
Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P., Capron A.
Mol. Biochem. Parasitol. 54:63-72(1992) [PubMed: 1518533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography."
Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M., Miele A.E., Trottein F., Brunori M., Bellelli A.
J. Mol. Biol. 360:678-689(2006) [PubMed: 16777141] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87799 Genomic DNA. Translation: AAA29892.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C80X-ray2.30A/B1-211[»]
2C8UX-ray2.00A/B1-211[»]
2CA8X-ray2.49A1-211[»]
2CAIX-ray2.26A/B1-211[»]
2CAQX-ray2.00A1-211[»]
2F8FX-ray2.10A/B1-211[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.18. 288876.

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.
IPR012336. Thioredoxin-like_fold.
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...

Other Resources

DrugBankDB00143. Glutathione.

Entry information

Entry nameGST28_SCHBO
AccessionPrimary (citable) accession number: P30113
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 1, 1994
Last modified: November 24, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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