IED ID | IndEnz0002000610 |
Enzyme Type ID | protease000610 |
Protein Name |
Pyrrolidone-carboxylate peptidase EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
Gene Name | pcp Rv0319 MTCY63.24 |
Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Enzyme Sequence | MSKVLVTGFGPYGVTPVNPAQLTAEELDGRTIAGATVISRIVPNTFFESIAAAQQAIAEIEPALVIMLGEYPGRSMITVERLAQNVNDCGRYGLADCAGRVLVGEPTDPAGPVAYHATVPVRAMVLAMRKAGVPADVSDAAGTFVCNHLMYGVLHHLAQKGLPVRAGWIHLPCLPSVAALDHNLGVPSMSVQTAVAGVTAGIEAAIRQSADIREPIPSRLQI |
Enzyme Length | 222 |
Uniprot Accession Number | P9WIJ5 |
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;Reference proteome;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 |