| IED ID | IndEnz0002014562 |
| Enzyme Type ID | protease014562 |
| Protein Name |
Probable Xaa-Pro aminopeptidase P AMPP Aminopeptidase P EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
| Gene Name | ampp BC1G_00838 |
| 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 | MESINTTERLAGLRELMKKNKVDIYIVPSEDSHSSEYIAACDARREFISGFSGSAGCAVVTLEKAALATDDNWLLLKQGLQDVPTWQEWAAEQSENGKVVGVDPTIMSASDARKLTEKIKKRGGNDLVAVEENLVDLVWGDSRPSRPKEPVKVLARKFAGKDVKTKLEDLRKELLKKKSSGLIVSMLDEIAWLFNLRGNDIPYNPVFFSYASVTSSSATLYVDSSKLSDECTAHLNENGVSVRDYSKIFGDAEVLSQSLDAEDTKVKKFLVSSRASWALKRALGGDAKVDEVRSPIGDAKSVKNETELEGMRACHVRDGAALIEYFAWLEHQLVVEKVKMDEVTAADRLEQLRSKQKNFVGLSFDTISSTGPNAAVIHYKPEPGNCSIIDPNAVYLCDSGAQYFDGTTDTTRTLHFGEPTEMEKKAYTLVLKGNIALDVAIFPKGTSGFALDVLARQFLWEEGLDYRHGTGHGVGSFLNVHEGPIGIGTRIQYSEVPLAPGNVISNEPGYYEDGSFGIRIENIIMVKEIETKHQFGEKPYLGFEHVTMVPYCRKLIDETLLTRKEKHWLNEYHADIYSKTKDFFKGDELTMSWLEREIEPL |
| Enzyme Length | 601 |
| Uniprot Accession Number | A6RK67 |
| 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 |
| 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 | 66,963 |
| Kinetics | |
| Metal Binding | METAL 398; /note=Manganese 2; /evidence=ECO:0000250; METAL 409; /note=Manganese 1; /evidence=ECO:0000250; METAL 409; /note=Manganese 2; /evidence=ECO:0000250; METAL 507; /note=Manganese 1; /evidence=ECO:0000250; METAL 521; /note=Manganese 1; /evidence=ECO:0000250; METAL 521; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |