Detail Information for IndEnz0002000508
IED ID IndEnz0002000508
Enzyme Type ID protease000508
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp CD630_16760
Organism Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Peptostreptococcaceae Clostridioides Clostridioides difficile (Peptoclostridium difficile) Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Enzyme Sequence MKILLTGFDPFGGEPINPAQEAVERVNNNINGAEIIKITIPTVMTKSVEAIDKTIQEHNPDIVISVGQAGGRFDITPERVAINIDDFRIKDNEGNQVIDTIIKEDGEPAYFSKLPVKAMVKHMNENKIPASVSNTAGTFVCNHVMYGILYMIDKKYPNIRGGFIHIPYTTSQVIDKKNTPFMSLEEIVKGLELAIEACIIYKEDVKEIGGEIS
Enzyme Length 213
Uniprot Accession Number Q186N3
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;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 23,592
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda