Detail Information for IndEnz0002000832
IED ID IndEnz0002000832
Enzyme Type ID protease000832
Protein Name Pyrrolidone-carboxylate peptidase
EC 3.4.19.3
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
PGP-I
Pyrase
Gene Name pcp VFMJ11_1451
Organism Aliivibrio fischeri (strain MJ11) (Vibrio fischeri)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Aliivibrio Aliivibrio fischeri (Vibrio fischeri) Aliivibrio fischeri (strain MJ11) (Vibrio fischeri)
Enzyme Sequence MKKILITGFEPFGNDKINPALEAVKLIAGRKLNGGEIVICQVPVVRYKSIETVKQAIEEQQPYAVITVGQASGRAAITPERIAINVDDFRIPDNEGIQVIDEPVVAGGPDAYFTTLPIKAMVSEIQAQGIPATVSNTAGTFVCNHLFYGIQHYLKDTNVRHGFVHIPLLPEQSVDGSQPTMKLEQIAEGLAIAAQAIIDNDSDIQQGAGTIC
Enzyme Length 212
Uniprot Accession Number B5FEA5
Absorption
Active Site ACT_SITE 80; /evidence=ECO:0000255|HAMAP-Rule:MF_00417; ACT_SITE 143; /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 22,804
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda