Detail Information for IndEnz0002000853
IED ID IndEnz0002000853
Enzyme Type ID protease000853
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp BSU02650
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MRKKVLITGFDPFDKETVNPSWEAAKRLNGFETEEAIITAEQIPTVFRSALDTLRQAIQKHQPDIVICVGQAGGRMQITPERVAINLADARIPDNEGHQPIDEEISPDGPAAYWTRLPVKRMTAKMKEHGIPAAVSYTAGTFVCNYLFYGLMDHISRTSPHIRGGFIHIPYIPQQTIDKTAPSLSLDTIVRALRIAAVTAAQYDEDVKSPGGTLH
Enzyme Length 215
Uniprot Accession Number P28618
Absorption
Active Site ACT_SITE 81; /evidence=ECO:0000250; ACT_SITE 144; /evidence=ECO:0000250; ACT_SITE 168; /evidence=ECO:0000250
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
Pathway
nucleotide Binding
Features Active site (3); Chain (1)
Keywords Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Thiol protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,774
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda