IED ID | IndEnz0002000838 |
Enzyme Type ID | protease000838 |
Protein Name |
Pyrrolidone-carboxylate peptidase EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
Gene Name | pcp |
Organism | Bacillus amyloliquefaciens (Bacillus velezensis) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus amyloliquefaciens group Bacillus amyloliquefaciens (Bacillus velezensis) |
Enzyme Sequence | MEKKVLLTGFDPFGGETVNPSWEAVKRLNGAAEGPASIVSEQVPTVFYKSLAVLREAIKKHQPDIIICVGQAGGRMQITPERVAINLNEARIPDNEGNQPVGEDISQGGPAAYWTGLPIKRIVEEIKKEGIPAAVSYTAGTFVCNHLFYGLMDEISRHHPHIRGGFIHIPYIPEQTLQKSAPSLSLDHITKALKIAAVTAAVHEDDIETGGGELH |
Enzyme Length | 215 |
Uniprot Accession Number | P46107 |
Absorption | |
Active Site | ACT_SITE 81; ACT_SITE 144; ACT_SITE 168 |
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; |
DNA Binding | |
EC Number | 3.4.19.3 |
Enzyme Function | FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Stable from pH 7.0 to 9.0.; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (7); Chain (1); Helix (6); Mutagenesis (2); Turn (1) |
Keywords | 3D-structure;Cytoplasm;Hydrolase;Protease;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1AUG; 3RNZ; 3RO0; |
Mapped Pubmed ID | 21875148; |
Motif | |
Gene Encoded By | |
Mass | 23,287 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |