P36267 · GGT_PSEUA
- ProteinGlutathione hydrolase proenzyme
- Geneggt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids575 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
Catalytic activity
- an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]
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 | 376 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 394 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 396 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 415 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 418 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 447-448 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: SS | ||||||
Binding site | 468-469 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: GG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | glutathione hydrolase activity | |
Molecular Function | leukotriene C4 gamma-glutamyl transferase activity | |
Biological Process | glutathione biosynthetic process | |
Biological Process | glutathione catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione hydrolase proenzyme
- EC number
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota
Accessions
- Primary accessionP36267
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MKNQTFSKALLATALSCALFNVHA | ||||||
Chain | PRO_0000011054 | 25-375 | Glutathione hydrolase large chain | |||
Sequence: ASQAPVGAENGMVVTAQHIASKVGVEVLKSGGNAIDAAVAVGYALAVVYPAAGNIGGGGFMTIQLADGRKTFLDFREKAPLAATANMYLDKDGNVIKGASTTGYLAVGVPGTVSGMEYAREKYGTKTRQQLISPAITLADKGFVLEQGDVDMLWTSTKDFEKDRANSGAIFMNKGQPFQPGERLVQKDLARTLRLISAKGTDGFYKGEVADKLVASMKAGGGIITQADLDQYKTRELAPVECDYRGYHVVSAPPPSSGGVVICEIMNILEGYPMKELGYHSAQGVHYTIEAMRHAYVDRNSYLGDPDFVKNPLAHLLDKDYAAKIRAAINPQKAGISQEIKPGVPPHEGSN | ||||||
Chain | PRO_0000011055 | 376-575 | Glutathione hydrolase small chain | |||
Sequence: TTHYSIVDKDGNAVSVTYTLNDWFGAKVMANGTGVLLNDEMDDFTSKVGVPNMYGLIQGEANAIGPGRRPLSSMSPTIVTKDGKTVMVVGTPGGSRIITATLLTMLNMIDYGMNLQEAVDAPRFHQQWMPESTNIEAFALSPDTQKILESWGQKFAGPQPANHIAAILVGAPSLGGKPIGKNRFYGANDPRRNTGLALGY |
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
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length575
- Mass (Da)61,301
- Last updated1994-06-01 v1
- ChecksumCF2EB69F02CD0201
Keywords
- Technical term