IED ID | IndEnz0002000742 |
Enzyme Type ID | protease000742 |
Protein Name |
Pyrrolidone-carboxylate peptidase EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
Gene Name | pcp YpsIP31758_1120 |
Organism | Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Yersinia Yersinia pseudotuberculosis complex Yersinia pseudotuberculosis Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) |
Enzyme Sequence | MRRVLITGFEPFGGERINPSWEVVKQMNDLMMGGVRIVARQLPCAFGEALTALNTAIDDVQPVLVLAIGQAGGRADITIERVAINVDDARIPDNLGNQPVDQPIIQEGPAAYFTRLPIKAMVQGIREAGIPASVSQTAGTYVCNHVMYGLLHRLNQFNNEVKGGFIHIPYLPEQAVDHPGAPSMSAQSVLVALELAISIALQIEHDLHITGGPVH |
Enzyme Length | 215 |
Uniprot Accession Number | A7FFS3 |
Absorption | |
Active Site | ACT_SITE 80; /evidence=ECO:0000255|HAMAP-Rule:MF_00417; ACT_SITE 143; /evidence=ECO:0000255|HAMAP-Rule:MF_00417; ACT_SITE 167; /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 | 23,168 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |