Detail Information for IndEnz0002000628
IED ID IndEnz0002000628
Enzyme Type ID protease000628
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp PYRAB14480 PAB1419
Organism Pyrococcus abyssi (strain GE5 / Orsay)
Taxonomic Lineage cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus abyssi Pyrococcus abyssi (strain GE5 / Orsay)
Enzyme Sequence MKVLVTGFEPFGGDDKNPTMEIVKFLDGKEIGGAKVIGRVLPVSFKRARKELVAILDEIKPDVTINLGLAPGRTHISVERVAVNIIDARIPDNDGEKPIDEPIVENGPAAYFATIPTREIVEEMKRNNIPAVLSYTAGTYLCNFVMYLTLHHSATKGYPRKAGFIHVPYTPDQVIEKKNTPSMSLELEIKGVEIAIRKSL
Enzyme Length 200
Uniprot Accession Number Q9UYQ9
Absorption
Active Site ACT_SITE 79; /evidence=ECO:0000250; ACT_SITE 142; /evidence=ECO:0000250; ACT_SITE 166; /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.
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.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,082
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda