Detail Information for IndEnz0002000595
IED ID IndEnz0002000595
Enzyme Type ID protease000595
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp BQ2027_MB0327
Organism Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium bovis Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Enzyme Sequence MSKVLVTGFGPYGVTPVNPAQLTAEELDGRTIAGATVISRIVPNTFFESIAAAQQAIAEIEPALVIMLGEYPGRSMITVERLAQNVNDCGRYGLADCAGRVLVGEPTDPAGPVAYHATVPVRAMVLAMRKAGVPADVSDAAGTFVCNHLMYGVLHHLAQKGLPVRAGWIHLPCLPSVAALDHNLGVPSMSVQTAVAGVTAGIEAAIRQSADIREPIPSRLQI
Enzyme Length 222
Uniprot Accession Number P0A5R5
Absorption
Active Site ACT_SITE 80; /evidence=ECO:0000250; ACT_SITE 146; /evidence=ECO:0000250; ACT_SITE 170; /evidence=ECO:0000250
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;
DNA Binding
EC Number 3.4.19.3
Enzyme Function FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. {ECO:0000250}.
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:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,193
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda