Detail Information for IndEnz0002000527
IED ID IndEnz0002000527
Enzyme Type ID protease000527
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp DR_0490
Organism Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Deinococcales Deinococcaceae Deinococcus Deinococcus radiodurans Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Enzyme Sequence MPTLLLTGFEPFHTHPDNPSAQAAQELHGLELPGGWGVHSALLPVEPHAAGAALTRLLSEQDPGAVLLTGLAAGRPQVTLERVGVGVMDFQIPDNAGQTYRDQPIEPDAPAAYLATLPLRAILAAWREAEIPGDISNSAGLYVCNFVLYHALHWLREHGRGAVPCGFLHVPANAAVALAVPADRPPLPYLPQSEITRAVRVAAEAITAQSSVLQMGKM
Enzyme Length 218
Uniprot Accession Number Q9RX25
Absorption
Active Site ACT_SITE 81; /evidence=ECO:0000250; ACT_SITE 144; /evidence=ECO:0000250; ACT_SITE 169; /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); Beta strand (9); Chain (1); Helix (7)
Keywords 3D-structure;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 X-ray crystallography (3)
Cross Reference PDB 5Z40; 5Z47; 5Z48;
Mapped Pubmed ID 30950401;
Motif
Gene Encoded By
Mass 23,096
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda