| IED ID | IndEnz0002016699 |
| Enzyme Type ID | protease016699 |
| Protein Name |
Probable Xaa-Pro aminopeptidase pepP EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
| Gene Name | pepP PTT_18417 |
| Organism | Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Pleosporaceae Pyrenophora Pyrenophora teres Pyrenophora teres f. teres Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres) |
| Enzyme Sequence | MAIAENYEDVLKGKYPAKAHAKKVAEWIIAKGGDKNGTIYLEAQKQKLNEDNDGEAPFRQRRYFFYLSGCELPDSYLTYEIATEKLTLFIPPVEPDEVIWSGLPMSPEDAKAKYDIDHCLTTKDVNAHLTSTSESAQSTIYAIPEQVSDHVTFISYKEKEFKQLKPAIEYCRVTKSDYEIALIRKANMISTAAHEAVMKAASTAKNECELEAVFLKACVERNAKNQAYHSIVAAGEHAATLHYVHNAAPISDQNLLLLDAGCEVDCYASDITRTFPLKGKFTAESLAIYKIVLDMQHQCINALKEGVVWDSVHELAHKVAIKGLLELGILKGDAEEIFTKRISVAFFPHGLGHYLGMDTHDTGGNANYADKDVMFRYLRTRGSLPERSVITVEPGVYFCRFIIEPYLKDEEKKKYIDESVLERYWSVGGVRIEDNVLVTKNGFENLTPTPKEIDDITKLILST |
| Enzyme Length | 463 |
| Uniprot Accession Number | E3S6N7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; |
| DNA Binding | |
| EC Number | 3.4.11.9 |
| Enzyme Function | FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome |
| 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 | 52,011 |
| Kinetics | |
| Metal Binding | METAL 259; /note=Manganese 2; /evidence=ECO:0000250; METAL 270; /note=Manganese 1; /evidence=ECO:0000250; METAL 270; /note=Manganese 2; /evidence=ECO:0000250; METAL 393; /note=Manganese 1; /evidence=ECO:0000250; METAL 433; /note=Manganese 1; /evidence=ECO:0000250; METAL 433; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |