| IED ID | IndEnz0002005635 |
| Enzyme Type ID | protease005635 |
| Protein Name |
Probable Xaa-Pro aminopeptidase PEPP EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
| Gene Name | PEPP HCDG_01478 |
| Organism | Ajellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Ajellomycetaceae Histoplasma Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum) Ajellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) |
| Enzyme Sequence | MDESVDRVLAGKYPAKAHAKRVAARIRELGYGESGVIYLEGQKTQMIEDNDGSMPFRQRRNFFYLSGCPLPDSYLTYNIEEDHLTLFIPPIDEDSVIWSGLPLSPDEALEMYDVDAVLLTTDVNTSLAHFCSVKKGKKVFALADQVSPHITFLPFQETDFDVLKRAAEESRVVKDTYEIALLRRANEISTKAHVAVIKAARSAANERELEAIFIATCMSYGCREQSYHPIFASGTNAATLHYQNNNEDLVDKTTGEKRLNMLVDAGGEYRTYCADITRVVPLSGKFSAESRQIYDIVLDMQMTSLAMIRAGVMWEDVHSNSHRVAIRGLLKLGILRGTEEELFDKGISVAFFPHGVGHYLGMDTHDTGGNPNYEDENPKFKYLRLRGTLACGAVVTVEPGIYFCRFIIDPYLASPELGKYIDTNVLERYWNVGGVRIEDNVVVTQNGHDNLTAAPKIPEEIEKLVAATQ |
| Enzyme Length | 469 |
| Uniprot Accession Number | C6H7R7 |
| 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 | 52,439 |
| Kinetics | |
| Metal Binding | METAL 264; /note=Manganese 2; /evidence=ECO:0000250; METAL 275; /note=Manganese 1; /evidence=ECO:0000250; METAL 275; /note=Manganese 2; /evidence=ECO:0000250; METAL 398; /note=Manganese 1; /evidence=ECO:0000250; METAL 438; /note=Manganese 1; /evidence=ECO:0000250; METAL 438; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |