IED ID | IndEnz0002016687 |
Enzyme Type ID | protease016687 |
Protein Name |
Probable Xaa-Pro aminopeptidase PEPP EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
Gene Name | PEPP GLRG_11122 |
Organism | Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Glomerellaceae Colletotrichum Colletotrichum graminicola species complex Colletotrichum graminicola (Maize anthracnose fungus) (Glomerella graminicola) Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) |
Enzyme Sequence | MTQDYETVLKGKYPAKEHALRVADYVKSKVPDATGILYVEGRMTKMLEDNDEPEPFRQRRYFYYLTGCPLADCHYIFDLATSKSTLFIPPIDPDSVIWSGLPVSAAEAKELYDVDEVKYTTDVNAELARLGKGPKKTVFAIQNQVLDSITFLEFDEKNFSILKDAIERCRVVKDDYEIALTRKANAVSTVAHHAVVEYVKKAKNERELEALFLQRSVANGAKNQAYHGIFAGGRAAATLHYVANDAPLEGKLNLLLDAGTEWNCYASDITRTFPISGKFSKESRQIYDIVLKMQLETTAALKEGVIWDEIHLLAHKIAIDGLHLIGILKGDKDEILKNRTSVAFFPHGLGHYLGMDTHDVGGNANYADRDPMFRYLRVRGALPAGSIVTVEPGIYFCSFIIEPYLKDPVHSKFIDSAVLEKYWDVGGVRIEDNILITKDGSENLTPTIKDPDELEKIIQAS |
Enzyme Length | 461 |
Uniprot Accession Number | E3QYP0 |
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 | 51,662 |
Kinetics | |
Metal Binding | METAL 257; /note=Manganese 2; /evidence=ECO:0000250; METAL 268; /note=Manganese 1; /evidence=ECO:0000250; METAL 268; /note=Manganese 2; /evidence=ECO:0000250; METAL 391; /note=Manganese 1; /evidence=ECO:0000250; METAL 431; /note=Manganese 1; /evidence=ECO:0000250; METAL 431; /note=Manganese 2; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |