| IED ID | IndEnz0002000703 |
| Enzyme Type ID | protease000703 |
| Protein Name |
Pyrrolidone-carboxylate peptidase EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
| Gene Name | pcp SSU98_0795 |
| Organism | Streptococcus suis (strain 98HAH33) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus suis Streptococcus suis (strain 98HAH33) |
| Enzyme Sequence | MKIIVTGFDPFGGEPINPALETIKSLPKTIAGAEIILVEIPTVFDKAADVLEEKMAEHLPDAVLCIGQAGGRVDLTPERIAINQDDARIPDNEGQQPIDRTIREDGQPAYFSTLPIKAMVEAIHRIGLPASVSNTAGTFVCNHLMYQALYLAEKQFPKTKAGFLHIPFLPEQVVDKPGLASMSLNDIVRGVEVAIGAIVEYRDKEDIKKGGGSTH |
| Enzyme Length | 215 |
| Uniprot Accession Number | A4W0R4 |
| Absorption | |
| Active Site | ACT_SITE 78; /evidence=ECO:0000255|HAMAP-Rule:MF_00417; ACT_SITE 141; /evidence=ECO:0000255|HAMAP-Rule:MF_00417; ACT_SITE 165; /evidence=ECO:0000255|HAMAP-Rule:MF_00417 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.; EC=3.4.19.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00417}; |
| DNA Binding | |
| EC Number | 3.4.19.3 |
| Enzyme Function | FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. {ECO:0000255|HAMAP-Rule:MF_00417}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Cytoplasm;Hydrolase;Protease;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00417}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,281 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |