Detail Information for IndEnz0002000837
IED ID IndEnz0002000837
Enzyme Type ID protease000837
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp BALH_2757
Organism Bacillus thuringiensis (strain Al Hakam)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus thuringiensis Bacillus thuringiensis (strain Al Hakam)
Enzyme Sequence MKTVLLTGFDPFGGESINPAWEVAKSLHEKTIGEYKIISKQVPTVFHKSISVLKEYIEELAPEFIICIGQAGGRTDITIERVAINIDDARIADNEGNQPVDVPVVEEGPAAYWSTLPMKAIVKKLQEEGIPASVSQTAGTFVCNHLFYGLMHELEKHDTKMKGGFIHIPFLPEQASNYPGQPSMSLSTIRKGIELAVEVTTTVEVDIVEIGGTTH
Enzyme Length 215
Uniprot Accession Number A0RFP3
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 23,531
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda