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Reviewed, UniProtKB/Swiss-Prot P30114 (GST28_SCHHA)

Last modified November 24, 2009. Version 62. 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):
    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.

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_0000185813

Regions

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

Sites

Active site101 Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30114-1 [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: 1518533] [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: 12939136] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), ACTIVE SITE TYR-10.
+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[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.18. 277766.

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...

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: November 24, 2009
This is version 62 of the entry and version 1 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