Detail Information for IndEnz0002003899
IED ID IndEnz0002003899
Enzyme Type ID protease003899
Protein Name Probable Xaa-Pro aminopeptidase P
AMPP
Aminopeptidase P
EC 3.4.11.9
Aminoacylproline aminopeptidase
Prolidase
Gene Name AMPP GLRG_03822
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 MERIDTTGRLSRLRELMKERNVDVYVIPSEDSHASEYIAGCDARREFISGFSGSAGCAVVTLDKAALATDGRYFNQASKQLDQNWLLLKQGLQDVPTWQEWSAEQSAGGKVVGVDPELITGSIAKKLTEKVKRSGGSDLVPLDENLVDLVWAEARPARPKNPIKVLPEKFSGKDVKTKLKELRQELDRKNSRAFVVSMLDEIAWLFNLRGDDIPYNPVFFSYAIITSDSATLYVDASKLGEETRAYLADNDVCVKPYDIVFDSINTLRSSDTSCQTTSGVSSKRFMISTKASWALKRSLGGDSQVDEVRSPIGDSKAVKNKSEMAGMRACHIRDGAALIEYFAWLEDQLVAKKVKLDEVQAADKLEQLRSKQKDYVGLSFDTISSTGANAAVIHYKPERGACSIIDPTAIYLCDSGAQYLDGTTDTTRTLHFGQPTEAEKLAYTLVLKGNIALDTAIFPKGTTGFAIDCLARQHLWKEGLDYRHGTGHGVGSYLNVHEGPIGIGTRVQFAEVALAPGNVLSIEPGFYEDGSYGIRIENVAMVTEVKTKHSFGDKPYLGFEHVTMVPYCRNLIEPNLLTAEEKAWLNAHHADILQKTKGYFQDDPLTMTWLARETQPL
Enzyme Length 617
Uniprot Accession Number E3QCU0
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 68,219
Kinetics
Metal Binding METAL 414; /note=Manganese 2; /evidence=ECO:0000250; METAL 425; /note=Manganese 1; /evidence=ECO:0000250; METAL 425; /note=Manganese 2; /evidence=ECO:0000250; METAL 523; /note=Manganese 1; /evidence=ECO:0000250; METAL 537; /note=Manganese 1; /evidence=ECO:0000250; METAL 537; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda