P09792 · GST28_SCHMA
- ProteinGlutathione S-transferase class-mu 28 kDa isozyme
- GeneGST28
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids211 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Miscellaneous
There are at least three isoenzymes of GST in S.mansoni.
Catalytic activity
- glutathione + RX = a halide anion + an S-substituted glutathione + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 10-11 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: YF | ||||||
Binding site | 16 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 41-45 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: WPKIK | ||||||
Binding site | 53 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 55-56 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: AV | ||||||
Binding site | 70-71 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: ES |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glutathione transferase activity | |
Biological Process | glutathione metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione S-transferase class-mu 28 kDa isozyme
- EC number
- Short namesGST 28
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Trematoda > Digenea > Strigeidida > Schistosomatoidea > Schistosomatidae > Schistosoma
Accessions
- Primary accessionP09792
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000185815 | 2-211 | Glutathione S-transferase class-mu 28 kDa isozyme | |||
Sequence: AGEHIKVIYFDGRGRAESIRMTLVAAGVDYEDERISFQDWPKIKPTIPGGRLPAVKVTDDHGHVKWMLESLAIARYMAKKHHMMGETDEEYYSVEKLIGQAEDVEHEYHKTLMKPQEEKEKITKEILNGKVPVLLNMICESLKGSTGKLAVGDKVTLADLVLIAVIDHVTDLDKGFLTGKYPEIHKHRENLLASSPRLAKYLSNRPATPF |
Keywords
- PTM
PTM databases
Expression
Tissue specificity
In the adult, expressed in excretory epithelial cells but absent from the caecal epithelium and flame cells. Also expressed in the tegument and its extensions into the parenchyma. In the schistosomulum, expressed in the tegument and associated structures. Not expressed in digestive tract, reproductive organs or muscles (at protein level).
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-86 | GST N-terminal | ||||
Sequence: EHIKVIYFDGRGRAESIRMTLVAAGVDYEDERISFQDWPKIKPTIPGGRLPAVKVTDDHGHVKWMLESLAIARYMAKKHHMMG | ||||||
Domain | 88-211 | GST C-terminal | ||||
Sequence: TDEEYYSVEKLIGQAEDVEHEYHKTLMKPQEEKEKITKEILNGKVPVLLNMICESLKGSTGKLAVGDKVTLADLVLIAVIDHVTDLDKGFLTGKYPEIHKHRENLLASSPRLAKYLSNRPATPF |
Sequence similarities
Belongs to the GST superfamily. Mu family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length211
- Mass (Da)23,820
- Last updated1989-07-01 v1
- ChecksumF988AAF041D767E3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 47 | in Ref. 6; AA sequence | ||||
Sequence: T → I | ||||||
Sequence conflict | 106 | in Ref. 6; AA sequence | ||||
Sequence: E → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X05148 EMBL· GenBank· DDBJ | CAA28796.1 EMBL· GenBank· DDBJ | mRNA | ||
M98271 EMBL· GenBank· DDBJ | AAA29891.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S71584 EMBL· GenBank· DDBJ | AAC60508.1 EMBL· GenBank· DDBJ | mRNA | ||
CABG01000068 EMBL· GenBank· DDBJ | CCD60449.1 EMBL· GenBank· DDBJ | Genomic DNA |