| IED ID | IndEnz0002003922 |
| Enzyme Type ID | protease003922 |
| Protein Name |
Probable Xaa-Pro aminopeptidase BC1G_13431 EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
| Gene Name | BC1G_13431 |
| Organism | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | MSSFTAQDKDQEVRPSSSGSWACKEVDEFDALSIEYKPKPTEKYPAKLHARNVRKYLDVGEGLIYLPGLPSFNYEDSDMPPAFRQRRYFYYITGVNLSDCIVTYNIHRDQLWLWIPPPNSGRSVIYNGARPTIKEIMSKYDFDHVETLTHLDSYLTWYAHTEPGKIHVLHDYQAPKNIELQITRKNGCHSIISESPFDSSKLEEAMNTARAIKSPYELRMIRKASAITAQGHLNVLRGLRHLSNEAEIEAIFTATCIAKQAKTQAYGVIAGSGENASTLHYMANNEPLKGRQLLCLDAGCEWDCYASDVTRTVPISGEYTEEAEAIYDIVAKMQDECIELLKPGANYRDIHIHAHKVALKGLMDLGLVEGGTFDELFMAGVSVAFFPHGLGHYVGLEVHDVGPGGSRITNRLYGFDKKPADWTDAYFQILSNTGVTSDGGSILEKDMVVTVEPGIYFSRYALEEVYLKSPNYAKYINKDLLQKYYPVGGVRIEDDLLITEDGYENLTTVLKGKEALKIINEGKEQEEEEEREANRKATESRKQKKTWFW |
| Enzyme Length | 549 |
| Uniprot Accession Number | A6SL16 |
| 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); Compositional bias (2); Metal binding (6); Region (2) |
| Keywords | Aminopeptidase;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease |
| 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 | 62,098 |
| Kinetics | |
| Metal Binding | METAL 297; /note=Manganese 2; /evidence=ECO:0000250; METAL 308; /note=Manganese 1; /evidence=ECO:0000250; METAL 308; /note=Manganese 2; /evidence=ECO:0000250; METAL 452; /note=Manganese 1; /evidence=ECO:0000250; METAL 493; /note=Manganese 1; /evidence=ECO:0000250; METAL 493; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |