IED ID | IndEnz0002000631 |
Enzyme Type ID | protease000631 |
Protein Name |
Pyrrolidone-carboxylate peptidase EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
Gene Name | pcp PF1299 |
Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus furiosus Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
Enzyme Sequence | MKVLVTGFEPFGGEKINPTERIAKDLDGIKIGDAQVFGRVLPVVFGKAKEVLEKTLEEIKPDIAIHVGLAPGRSAISIERIAVNAIDARIPDNEGKKIEDEPIVPGAPTAYFSTLPIKKIMKKLHERGIPAYISNSAGLYLCNYVMYLSLHHSATKGYPKMSGFIHVPYIPEQIIDKIGKGQVPPSMCYEMELEAVKVAIEVALEELL |
Enzyme Length | 208 |
Uniprot Accession Number | O73944 |
Absorption | |
Active Site | ACT_SITE 79; ACT_SITE 142; ACT_SITE 166 |
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); Beta strand (9); Chain (1); Disulfide bond (1); Helix (7) |
Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Reference proteome;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (9) |
Cross Reference PDB | 1IOF; 1IOI; 1X10; 1X12; 1Z8T; 1Z8W; 1Z8X; 2DF5; 2EO8; |
Mapped Pubmed ID | 16752900; 17510955; |
Motif | |
Gene Encoded By | |
Mass | 22,822 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.19.3; |