IED ID | IndEnz0002005602 |
Enzyme Type ID | protease005602 |
Protein Name |
Probable Xaa-Pro aminopeptidase P AMPP Aminopeptidase P EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
Gene Name | ampp PTRG_01084 |
Organism | Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Pleosporaceae Pyrenophora Pyrenophora tritici-repentis Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis) |
Enzyme Sequence | MAKVDTSHRLAELRKLMKERNVDIYTYISGFTGSAGYAVITHDKAALSTDGRYFNQAEKQLDSNWELLKQGIQDVPTIQEWTADQAEGGKVVGVDPSVVTAGDARKLAEKIKKKGGEYKAIDENLVDLVWSSERPARPSEKVIVQPERYACKGFEDKIDDLRKELEKKKSLGFVVSMLDEVAWLFNLRGSDIPYNPVFFSYAVVTPTAATLYVDENKLPEDVKEHLGNKITIRPYEAIFGDVTALSKELFEASDKNETQKKFLTSNRASWALNKALGGDDKVEETRSPVGDSKAVKNEVELEGMRQCHIRDGAALSEYFAWLEDQLINKKATLDEVDGADKLEEIRKKHDMFMGLSFDTISSTGANAAVIHYKPEKGECATIDPKAIYLCDSGAQYRDGTTDTTRTLHFTEPTEMERKAYTLVLKGNMALERVKFPKGTTGFALDALARQFLWAEGLDYRHGTGHGVGSFLNVHEGPIGIGTRVQYSEVSLAVGNVVSDEPGYYEDGKFGIRIENMVMVKEVETKHKFGDKPYLGFEHVTMTPHCRNLVDMSLLTEDEKKFINEYHKEVYEKTSKYFENDALTLEWLKRETAPY |
Enzyme Length | 594 |
Uniprot Accession Number | B2VUU7 |
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 | 66,842 |
Kinetics | |
Metal Binding | METAL 391; /note=Manganese 2; /evidence=ECO:0000250; METAL 402; /note=Manganese 1; /evidence=ECO:0000250; METAL 402; /note=Manganese 2; /evidence=ECO:0000250; METAL 500; /note=Manganese 1; /evidence=ECO:0000250; METAL 514; /note=Manganese 1; /evidence=ECO:0000250; METAL 514; /note=Manganese 2; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |