IED ID | IndEnz0002000575 |
Enzyme Type ID | protease000575 |
Protein Name |
Pyrrolidone-carboxylate peptidase EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
Gene Name | pcp LJ_1798 |
Organism | Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus johnsonii Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) |
Enzyme Sequence | MKILVTGFDPFGGDKINPAIEAVKRLPAEINGAEIIKLEIPTVFNKSAEVVKKAIEKEKPDYVLNVGQAGGRFGLTPERVAININDGRIPDNEGYQPLGEPIHEDGETAYFTQLPIKAEAKAIRDAGLPASVSNTAGTYVCNHIMYQVQYMRDKEFPNIKAGFIHIPFLPEQVVNRPNTPSMALGDIVKGLTAALSAIVERDGKGDIKAVEGANH |
Enzyme Length | 215 |
Uniprot Accession Number | Q74HE9 |
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;Reference proteome;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 | 23,289 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |