A0A7W7Z040 · A0A7W7Z040_9BRAD
- ProteinGlutathione hydrolase proenzyme
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids587 (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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 121 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 399 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 417-419 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TLN | ||||||
Binding site | 441 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 470-471 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: SS | ||||||
Binding site | 492 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: G |
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 > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Rhodopseudomonas
Accessions
- Primary accessionA0A7W7Z040
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-34 | |||||
Sequence: MVRLSPPRSRSVLRLVCCSVVTALLGLVGAGAQA | ||||||
Chain | PRO_5030758679 | 35-587 | Glutathione hydrolase proenzyme | |||
Sequence: QDIRGGAMPAAVAPAVAGARGMVVAQERLAATIGRDVLAKGGNAVDAAVATGFALAVTYPRAGNLGGGGFMVIHRVKENDDIALDYRETAPAAATRNMFLGPDGKPDNAKSRDSALGIGVPGTVAGLALALQKYGSGKFTLADILQPAIALARDGFVIADDTADTLPDWHKRLARWPATQKIFSRADGTSLQGGDKLVQHDLAATLGAIADQGPNGFYQGEVAEKLARGISDAGGIITPADLKAYQPVLRAPLRGTYRGYDIVAMPLPSSGGTVLIESLNILEGFQLRELPQGSAASLHLLIEAMKRGYADRARYLGDPAFVDAPLAALLSKDYATKQRAGIDPDRATPWTDALPALPPREGENTTHYSVVDADGNAVSNTYTLNFSYGLGLVADGTGVLLNNELDDFTAAPGASNAFGLVGFEANLPGPGKRPLSSMSPTLVLKNGRVVLVTGSPGGSRIISTTLQVIVDVLDYNMDIAAAVAAPRLHHQWLPDEVRIEHGFPEAVIAALRAKGHVVVAPLGQTSANSIFVAKDGVRGAPDPRTRGAAAVAE |
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
- Length587
- Mass (Da)60,936
- Last updated2021-06-02 v1
- Checksum0B11898C37680BCB
Keywords
- Technical term