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P30114 (GST28_SCHHA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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):
Sh28GST
OrganismSchistosoma haematobium (Blood fluke)
Taxonomic identifier6185 [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. Ref.2

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. Ref.2

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.2

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.

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_0000185813

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30114 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 954B2B60AA22E2C8

FASTA21123,960
        10         20         30         40         50         60 
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG GRLPAVKITD 

        70         80         90        100        110        120 
NHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYNVEKLIG QVEDLEHEYH KTLMKPEEEK 

       130        140        150        160        170        180 
QKITKEILNG 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]"Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium."
Johnson K.A., Angelucci F., Bellelli A., Herve M., Fontaine J., Tsernoglou D., Capron A., Trottein F., Brunori M.
Biochemistry 42:10084-10094(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87800 Genomic DNA. Translation: AAA29893.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OE7X-ray1.80A/B1-211[»]
1OE8X-ray1.65A/B1-211[»]
ProteinModelPortalP30114.
SMRP30114. Positions 4-211.
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

EvolutionaryTraceP30114.

Entry information

Entry nameGST28_SCHHA
AccessionPrimary (citable) accession number: P30114
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 76 of the entry and version 1 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