Detail Information for IndEnz0002000670
IED ID IndEnz0002000670
Enzyme Type ID protease000670
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp SH0293
Organism Staphylococcus haemolyticus (strain JCSC1435)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus haemolyticus Staphylococcus haemolyticus (strain JCSC1435)
Enzyme Sequence MKILVTAFDPFGGEKINPALEAVKQLENTIGEHTISKLEIPTVFHESKDVIDKELANGNYDVVLSIGQAGGRYDLTPERVGINIDDARIPDNKGNQPIDVAIQEDGAPAYFSNLPVKTMTEAIKAAGVPASLSNTAGTFVCNHVLYQLGYLADKSYPGLLFGFIHVPFIPEQVTDKPEKPSMSIETIAKGLTAAIKAISKEDDAKVALGETH
Enzyme Length 212
Uniprot Accession Number Q4L9S3
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;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 22,789
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda