| IED ID | IndEnz0002016147 |
| Enzyme Type ID | protease016147 |
| Protein Name |
Glutathione hydrolase proenzyme EC 3.4.19.13 Gamma-glutamyltranspeptidase proenzyme EC 2.3.2.2 Cleaved into: Glutathione hydrolase large chain; Glutathione hydrolase small chain |
| Gene Name | ggt |
| Organism | Pseudomonas sp. (strain A14) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Proteobacteria incertae sedis unclassified pseudomonads Pseudomonas sp. (strain A14) |
| Enzyme Sequence | MKNQTFSKALLATALSCALFNVHAASQAPVGAENGMVVTAQHIASKVGVEVLKSGGNAIDAAVAVGYALAVVYPAAGNIGGGGFMTIQLADGRKTFLDFREKAPLAATANMYLDKDGNVIKGASTTGYLAVGVPGTVSGMEYAREKYGTKTRQQLISPAITLADKGFVLEQGDVDMLWTSTKDFEKDRANSGAIFMNKGQPFQPGERLVQKDLARTLRLISAKGTDGFYKGEVADKLVASMKAGGGIITQADLDQYKTRELAPVECDYRGYHVVSAPPPSSGGVVICEIMNILEGYPMKELGYHSAQGVHYTIEAMRHAYVDRNSYLGDPDFVKNPLAHLLDKDYAAKIRAAINPQKAGISQEIKPGVPPHEGSNTTHYSIVDKDGNAVSVTYTLNDWFGAKVMANGTGVLLNDEMDDFTSKVGVPNMYGLIQGEANAIGPGRRPLSSMSPTIVTKDGKTVMVVGTPGGSRIITATLLTMLNMIDYGMNLQEAVDAPRFHQQWMPESTNIEAFALSPDTQKILESWGQKFAGPQPANHIAAILVGAPSLGGKPIGKNRFYGANDPRRNTGLALGY |
| Enzyme Length | 575 |
| Uniprot Accession Number | P36267 |
| Absorption | |
| Active Site | ACT_SITE 376; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 100; /note=Glutamate; /evidence=ECO:0000250; BINDING 394; /note=Glutamate; /evidence=ECO:0000250; BINDING 396; /note=Glutamate; /evidence=ECO:0000250; BINDING 415; /note=Glutamate; /evidence=ECO:0000250; BINDING 418; /note=Glutamate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000269|PubMed:7765305}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; Evidence={ECO:0000269|PubMed:7765305}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; Evidence={ECO:0000269|PubMed:7765305}; |
| DNA Binding | |
| EC Number | 3.4.19.13; 2.3.2.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Sulfur metabolism; glutathione metabolism. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (5); Chain (2); Region (2); Signal peptide (1) |
| Keywords | Acyltransferase;Direct protein sequencing;Glutathione biosynthesis;Hydrolase;Periplasm;Protease;Signal;Transferase;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and a small subunit. |
| Signal Peptide | SIGNAL 1..24 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 61,301 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23904; RHEA:28807; RHEA:59468 |
| Cross Reference Brenda |