Detail Information for IndEnz0002000615
IED ID IndEnz0002000615
Enzyme Type ID protease000615
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp ECA1354
Organism Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Pectobacterium Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica) Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Enzyme Sequence MKTVLITAFEPFEGEAINPSWEAVKDLHQREVGGVRVVACRLSCVFDLSLDQLYRAIAEWQPEVVIAVGQAGGRADISVERVAININDARIADNRGNQPIDTPVVEKGPAAYFSTLPVKALVQALHVAGIPASVSQTAGTFVCNHVMYGLLHQLHQQGDVVRGGFVHIPYSPEQAARHPGEPSMPTPLVTAALEVMIKQLLVQQVDVAITGGALH
Enzyme Length 215
Uniprot Accession Number Q6D7H1
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;Reference proteome;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 23,095
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda