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P30113 (GST28_SCHBO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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 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. Ref.2

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence AAA29892.1 differs from that shown. Reason: Erroneous initiation.

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

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

Regions

Domain4 – 8683GST N-terminal
Domain88 – 211124GST C-terminal
Region41 – 455Glutathione binding
Region70 – 712Glutathione binding

Sites

Binding site101Glutathione
Binding site161Glutathione
Binding site531Glutathione; via amide nitrogen and carbonyl oxygen

Experimental info

Mutagenesis101Y → F: Loss of enzyme activity. Ref.2
Mutagenesis211R → L: Reduces catalytic activity 12-fold. Ref.2
Mutagenesis211R → Q: Reduces catalytic activity 120-fold. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30113 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, MUTAGENESIS OF TYR-10 AND ARG-21.

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[»]
ProteinModelPortalP30113.
SMRP30113. Positions 4-211.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00143. Glutathione.

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

EvolutionaryTraceP30113.

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: April 16, 2014
This is version 80 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