| IED ID | IndEnz0002010925 |
| Enzyme Type ID | protease010925 |
| Protein Name |
Prolyl oligopeptidase A EC 3.4.21.26 |
| Gene Name | POPA |
| Organism | Amanita bisporigera (Destroying angel) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Amanitaceae Amanita Amanita bisporigera (Destroying angel) |
| Enzyme Sequence | MHRFLQPVRERLRSALARYFGSRIMSSTQWTPNMYPSARRSDHIDTYRSETRGEVKVPDPYHWLEEYSEETDKWTSDQEEFTRTYLDSNPDRKKLEDAFRKSMDYPKFSAPFLNDDKRWYWFYNTGLQAQTVICRSKDETLPDFSESDYVGETFFDPNLLSSDGTASLSMYDFSHCGKYFAYGISLSGSDFSTIYVRSTSSPLAPGNNSIRNDDGRLPDELRYVKFSSISWTKDSKGFFYQRYPGTGTVNGQNGIQTQGDRDAMIYYHRIGTSQSDDILVHEDQEHPDWVFGAEVTEDGKYVALYTMKDTSRKNLLWIADLGQNEVGRNMKWNKICNVFDSEYDLIGNDGSLLYIRTNKAAPQYKIVTLDIEKPELGFKEFIPEDPKAYLSQVKIFNKDRLALVYKRNVIGELYVYNNTGSRLMRLARDFVGSMTVTARETEPWFFATLTGFNTPGIVCRYNIQRPEEQRWSVYRTAKVKGLNPNDFEARQVWYDSYDGTKIPMFIVRHKNTQFNGTAPAIQYGYGGFNISINPFFSPTILTFLQKYGAILAVPNIRGGGEFGETWHDAGIREKRANVYDDFIAATQFLVKNKYAAGGKVAINGGSNGGLLVAACVNRAREGTFGAAIAEVGVLDLLKFPKFTIGKAWISDYGDPEDPRDFDYIYTHSPLHNIPKNMVLPPTMLLTADHDDRVVPMHSFKYAAMLQYTLPHNRHPLLLRVDKKAGHGGGKSTEKRLQEAADKWGFAAQSMGLAWKDRQANL |
| Enzyme Length | 761 |
| Uniprot Accession Number | E2JFG1 |
| Absorption | |
| Active Site | ACT_SITE 606; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 690; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 726; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000305}; |
| DNA Binding | |
| EC Number | 3.4.21.26 |
| Enzyme Function | FUNCTION: Housekeeping prolyl oligopeptidase (POP) that behaves like a conventional POP by cleaving peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long (By similarity). {ECO:0000250|UniProtKB:H2E7Q7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Hydrolase;Protease;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 86,914 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.26; |