Detail Information for IndEnz0002000504
IED ID IndEnz0002000504
Enzyme Type ID protease000504
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp CLL_A1534
Organism Clostridium botulinum (strain Eklund 17B / Type B)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium botulinum Clostridium botulinum B Clostridium botulinum (strain Eklund 17B / Type B)
Enzyme Sequence MKVLITGFDPFGGESINPALEAVKKLPNTISNAEIIKLEIPTVFKKSLDKIEENILAHKPDILISIGQAGGRFGITPERVAINIDDARIQDNEKNQPIDLKVFEDGENAYFTTLPIKAMVKEMQEAGIPSSVSNSAGTFVCNHVMYGVLYMINKKYPNIKGGFIHVPYIPSQVVNKPNMPSMSIEDISKGLELSVKAAVENNTDIKTAQGEIC
Enzyme Length 213
Uniprot Accession Number B2TK93
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;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 23,302
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda