| IED ID | IndEnz0002014169 |
| Enzyme Type ID | protease014169 |
| Protein Name |
Probable Xaa-Pro aminopeptidase pepP EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
| Gene Name | pepP Pc13g05440 |
| Organism | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium rubens Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
| Enzyme Sequence | MTTVDTILAAKYPAKAHALRVSESLKARHGGAGVIYLEAQKTRLIEDSDEDMPFRQRRPFFYLTGCLLPDAAVVYDAVKDELTLFIPPINPESVIWSGLPLSPEEAAKLYDVDRVLFTTDVNSTLASIASSHNGQTAAFAIAEQVSEGTSFQGFAETNTTSLKTAIEETRVIKDAYEVALLRKANDISTKAHVAAIHASKTATNERQIEAAIIGACIANGCREQSYHPIVAGGEGGATLHYVRNDVDLVDPVTKQRKNNVLIDAGGEYQTYCADITRVIPLNGRFAPETRQIYEIVLQMQTECIAMLKEGVCWDDVHALAHRIAIRGLLKLGILRGSEDELFEKRVSVAFFPHGLGHYLGMDTHDTGGNPNYEDKDTMFRYLRVRANLPAGSVVTVEPGIYFCRFIIDPILKAPETGKYIDTEVLERYWSVGGVRIEDNIHITKDGSENLTTAPKSIEEVESLAL |
| Enzyme Length | 465 |
| Uniprot Accession Number | B6H2M0 |
| 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 | 51,201 |
| Kinetics | |
| Metal Binding | METAL 263; /note=Manganese 2; /evidence=ECO:0000250; METAL 274; /note=Manganese 1; /evidence=ECO:0000250; METAL 274; /note=Manganese 2; /evidence=ECO:0000250; METAL 397; /note=Manganese 1; /evidence=ECO:0000250; METAL 437; /note=Manganese 1; /evidence=ECO:0000250; METAL 437; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |