IED ID | IndEnz0002003654 |
Enzyme Type ID | protease003654 |
Protein Name |
Probable Xaa-Pro aminopeptidase P AMPP Aminopeptidase P EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
Gene Name | AMPP MCYG_01718 |
Organism | Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Microsporum Arthroderma otae (Microsporum canis) Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
Enzyme Sequence | MTLFRSHLRFLFKPRFLYFQSPTGQSSRPFSTSQILRTALDMPPPPVDTTQRLAKLRELMKQNKVDVYIVPSEDSHQSEYIAPCDGRRAFISGFTGSAGCAIVSMSKAALSTDGRYFSQAAKQLDANWKLLKRGVEGVPTWEEWTAEQAENGKVVGVDPSLITAADARKLSQTLKATGGSLVGIDQNLIDIVWGDERPARPVTTITVQPVELAGKPFEEKVEALRKELATKKRSAMVISAEIYVDDSRLSPEARKQLEGKVVLKPYDAIFQASKVLAESKASASDGAASGKFLLSNKASWSLSLALGGEQNVDEVRSPITDAKAIKNDVELEGFRKCHIRDGAALIEYFAWLENALIKEGAKLDEVDGADKLYEIRKKYDLFVGNSFDTISSTGANGAIIHYKPEKSTCSVIDPKAMYLCDSGGQYKDGTTDTTRTLHFGEPTEFQKKAYALVLKGHISIDNAIFPKGTTGYAIDSFARQHLWREGLDYLHGTGHGVGSFLNVHEGPMGIGSRAQYAEVPLSAKNVLSNEPGYYEDGNFGIRLENLVICKEVETTHKFGDKPFLGFEYITMVPFCQKLLDASLLTEAERKWVNDYHAKVWEKTSPFFEKDELTLNWLKRETQPI |
Enzyme Length | 624 |
Uniprot Accession Number | C5FHR9 |
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 | 69,198 |
Kinetics | |
Metal Binding | METAL 421; /note=Manganese 2; /evidence=ECO:0000250; METAL 432; /note=Manganese 1; /evidence=ECO:0000250; METAL 432; /note=Manganese 2; /evidence=ECO:0000250; METAL 530; /note=Manganese 1; /evidence=ECO:0000250; METAL 544; /note=Manganese 1; /evidence=ECO:0000250; METAL 544; /note=Manganese 2; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |