Detail Information for IndEnz0002000751
IED ID IndEnz0002000751
Enzyme Type ID protease000751
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp YpAngola_A3594
Organism Yersinia pestis bv. Antiqua (strain Angola)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Yersinia Yersinia pseudotuberculosis complex Yersinia pestis Yersinia pestis bv. Antiqua (strain Angola)
Enzyme Sequence MRRVLITGFEPFGGERINPSWEVVKQMNDLMMGGVRIVARQLPCAFGEALTALNTAIDDVQPVLVLAIGQAGGRADITIERVAINVDDARIPDNLGNQPVDQPIIQEGPAAYFTRLPIKAMVQGIREAGIPASVSQTAGTYVCNHVMYGLLHRLNQFNNEVKGGFIHIPYLPEQAVDHPGAPSMSAQSVLVALELAISIALQIEHDLHITGGAVH
Enzyme Length 215
Uniprot Accession Number A9R3Y5
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 23,142
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda