A0A1E3UVJ4 · A0A1E3UVJ4_9GAMM
- ProteinGlutathione hydrolase proenzyme
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids570 (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.
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 > Gammaproteobacteria > Alteromonadales > Shewanellaceae > Shewanella
Accessions
- Primary accessionA0A1E3UVJ4
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MIKTIKSICTLVTVATAMSSSGVLA | ||||||
Chain | PRO_5009137591 | 26-570 | Glutathione hydrolase proenzyme | |||
Sequence: MDRITGKAFATRSEVYATHGMAATSQPLATQVAIDVLKQGGSAVDAAIAANAMLGLVEPTGSGVGGDLFAIVWSAKDKKLYGLNASGRSPKSLTLEKLKSLGLDYLPPLGPLPVSVPGAVDGWFELHDKFGKLPMADNLAPAIRYAREGFPVSELIAYYLEGSGKKLAQFPGFKETYMPNGKMPAVGEIFKNPALANTYEKIAKGGRDAFYKGDIAKSIDKYIKAQGGYLSYEDLASHTSDWIEPVSVNYRGYDVWELPPNGQGIAALQILKTMEPFDVATMGFNSPEYVHLFVEAKKLAFADRAKFYADMAFNKVPVKELISQQYNYDRAKLIDLNKAAKSVDAGNPALQHGDTVYLTTADKDGNMVSLIQSNYRGMGSGMTPPDLGFVLQDRGQMFDLTEGRFNTYAPGKRPFHTIIPAFVTKDGKPWLSFGVMGGATQPQMHAQIIINLIDFKMNLQEAGDAPRILHSGSTEPTGEIMNDGGYVSLESGFPVETRRELMKKGHVLRDVLGDFGGYQAIGFNAETGVYRGASESRKDGYAAGY |
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.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length570
- Mass (Da)61,614
- Last updated2017-01-18 v1
- ChecksumE0A7F207B55189A8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LDOA01000001 EMBL· GenBank· DDBJ | ODR84606.1 EMBL· GenBank· DDBJ | Genomic DNA |