A0A4S1GXU9 · A0A4S1GXU9_UNCXX
- ProteinGlutathione hydrolase proenzyme
- Geneggt
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids536 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Pathway
Sulfur metabolism; glutathione metabolism.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 359 | Nucleophile | |||
Binding site | 418-419 | L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 440 | L-glutamate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glutathione hydrolase activity | |
Molecular Function | leukotriene C4 gamma-glutamyl transferase activity | |
Biological Process | glutathione biosynthetic process | |
Biological Process | glutathione catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione hydrolase proenzyme
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria
Accessions
- Primary accessionA0A4S1GXU9
Proteomes
PTM/Processing
Post-translational modification
Cleaved by autocatalysis into a large and a small subunit.
Keywords
- PTM
Interaction
Subunit
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
Structure
Sequence
- Sequence statusComplete
- Length536
- Mass (Da)58,102
- Last updated2019-07-31 v1
- MD5 ChecksumA893DC9770151F69ECEE72819DBD5558
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SRTJ01000008 EMBL· GenBank· DDBJ | TGV44407.1 EMBL· GenBank· DDBJ | Genomic DNA |