A0A6G8CI33 · A0A6G8CI33_9BURK
- ProteinGlutathione hydrolase proenzyme
- Geneggt
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids654 (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 binding site, active site.
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 > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Diaphorobacter
Accessions
- Primary accessionA0A6G8CI33
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-28 | |||||
Sequence: MQTRKLWPLAPMAIAVLLVGCNSSNHHD | ||||||
Chain | PRO_5026296333 | 29-654 | Glutathione hydrolase proenzyme | |||
Sequence: DENELRVDTDAKSCTVLSSSGGSVVVGSGVTGDPAAPEAASGYRLGLKAKQSNSYMAVANTPLASKAGCEVLKAGGTAVDAAVAMQAVLGLVEPQSSTIAGSAFMVYYDAKTKKVVAYDGRESAPAAATGYYLARQDQADPNSSAPVPSARRSGRSIGVPGVLRMLEMAQKEHGRLAWNGLFDSGIKLADDGFKIPGRLGDAIKSNATSLALDSNAMATYFKADGTPRLTGEVMTNKPYAATLRTIASKGADGLHTGDIAKNIVAKAAQSVGDDAAKTPITPSLMTLDDLANYKAKKRDPVCVNYRGTYHVCTMSPPSSGGIAIAQGLGILSQFNMAQYAPMNPTNEGGVPSVMGVHLLTEAERLAYADRDKYVADTDFIPLPGSGVPTLLNADYLKARAALINPDKSMGTAQAGDLGTVPLGVDKTVEHGTTHLSVVDAYGNVVSMTTTVESSMGSFHMVNGFLLTNQLTDFSAAPVDSAGTPIANRVAPGKRPRSTMAPTLVFKGDKPGDFVMATGSPGGGAIIQYVMKTVVGALDWGLDAQQATSLVNTGASNSATTGIDGSNTSLDLTALVDGLKAKGHTVNTAAQSSGVATIIRVTKDGKSVLQGGADPRREGIVLGDGAL |
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
- Length654
- Mass (Da)67,369
- Last updated2020-08-12 v1
- Checksum8C86A3B42CFBC3AF
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP049910 EMBL· GenBank· DDBJ | QIL78521.1 EMBL· GenBank· DDBJ | Genomic DNA |