| IED ID | IndEnz0002005643 |
| Enzyme Type ID | protease005643 |
| Protein Name |
Probable Xaa-Pro aminopeptidase pepP EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
| Gene Name | pepP AFUA_2G07500 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MMAAVDAILAGKYPAKAHARRVAESLQSYRNGCPGIVYLEAQKTRLIEDNDEPAPFRQRRPFFYLSGCPLPDSCLVYDLSEDQLTLFIPPVDPEDVIWSGLPMSTEEAQNQYDVDRVLVTTELNSTLASIVSSHGGKAIAFTIADQVSESTQFHGFSEVNHSVLKGVIEQSRVVKDEYEVALLRKANDISAKAHIAAIKASQTAVNEREIEGAFIATCIANGAREQSYHPIVACGENGATLHYGKNDDTLIDPVTNQKKRNVLIDAGGEYRTYCADITRVIPVGGKFTAETRQIYDIVLQMQTECIAMLKEGVQWEDVHAHAHRVAIRGLLKLGILRGAEDEIFEKRVSVAFFPHGLGHYLGMDTHDTGGNPNYADKDTMFRYLRVRGRLPAGSVITVEPGVYFCRFIIEPYIKSPESNKYIDTNVLDRYWRVGGVRIEDNVLVTKDGYDNLTTAPKAVDELERLAAS |
| Enzyme Length | 468 |
| Uniprot Accession Number | Q4X267 |
| 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 | 51,944 |
| Kinetics | |
| Metal Binding | METAL 265; /note=Manganese 2; /evidence=ECO:0000250; METAL 276; /note=Manganese 1; /evidence=ECO:0000250; METAL 276; /note=Manganese 2; /evidence=ECO:0000250; METAL 399; /note=Manganese 1; /evidence=ECO:0000250; METAL 439; /note=Manganese 1; /evidence=ECO:0000250; METAL 439; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |