A0A9E0SPF7 · A0A9E0SPF7_UNCPS
- ProteinGlutathione hydrolase proenzyme
- Geneggt
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids574 (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 | 100 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 375 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 393-395 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TLN | ||||||
Binding site | 417 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 446-447 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: SS | ||||||
Binding site | 468 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | acyltransferase activity | |
Molecular Function | glutathione hydrolase 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
Accessions
- Primary accessionA0A9E0SPF7
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MLTTTHRIALIASVTAFACGAVEA | ||||||
Chain | PRO_5038802774 | 25-574 | Glutathione hydrolase proenzyme | |||
Sequence: ASQAPVAAEHGMVVSAQHLATQVGVDVLKEGGNAIDAAVAVGYALAVVYPAAGNLGGGGFMTIQLADGRKTFLDFREKAPLGATPNMYLDKDGNVIKGASTTGHLAVGVPGTVSGLETARAKYGTLPRKALIAPAIAYAERGFTLDQGDVDLLVTSTDDFKKDPASAPIFLNKGEAFQPGQKLVQKDLAKTLQAISDKGEDGFYKGWVGSAIVASSQAGKGLITQADLDQYKTRELAPVECDYRGFHVVSAPPPSSGGVVICEILNVLEGYPLKDLGFRSAQAVQYQIEAMRHAYVDRNSYLGDPDFVKNPLDRLLSKDYAAKIRGVIEPNKAGISKDIKPGVAPHEGSNTTHYSIVDQMGNAVSVTYTLNDWFGAKVLAAGTGVLLNDEMDDFTAKVGVPNLYGLVQGEANKVEPGKRPLSSMSPTIVTKDGKPVMVVGTPGGSRIITAVLHTIINVIDYGMNVQEAVDAPRFHQQWLPETTNIETFALSPDTKKILEGWGQKFSGPQPANHVAAILVGAPTLGGKPVGNNKFYGANDPRRNSGLALGY |
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
- Length574
- Mass (Da)60,529
- Last updated2023-05-03 v1
- Checksum1AC41A281110A658