Detail Information for IndEnz0002000838
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