Detail Information for IndEnz0002016652
IED ID IndEnz0002016652
Enzyme Type ID protease016652
Protein Name Probable Xaa-Pro aminopeptidase P
AMPP
Aminopeptidase P
EC 3.4.11.9
Aminoacylproline aminopeptidase
Prolidase
Gene Name AMPP Lema_P022290
Organism Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Leptosphaeriaceae Leptosphaeria Leptosphaeria maculans species complex Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) Leptosphaeria maculans 'brassicae' group Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
Enzyme Sequence MAKVDTTERLAELRKLMKERNVDIYMVPSEDSHQSEYIAPCDARRGSAGYAVITHDKAALATDGRYFNQAEKQLDGNWELLKQGIQDVPTIQDWTADQVEGGKVVAVDPSVVTAADARKLADKIKKKGGEYKAVDDNLVDKIWSDRPSRPHEKVIVQPIEFSGKSFEDKIEDLRKELEKKKSLGFVVSMLDEIAWLFNLRGSDIPYNPVFFSYAVVTPTTVTLYVDDHKLPEEVKKHLGDKVTIRPYNAIFEELTTLSKEAFTKDKADATSKFLTSSRASWALNKALGGEDRVEETRSPVGDAKAVKNEVELEGMRQCHLRDGAALSEYFAWLEDQLINKKAELDEVDGADKLEAIRKKHDKFMGLSFDTISSTGANAAVIHYKPEKGECAVIDAKAIYLCDSGAQYRDGTTDTTRTVHFTEPTEMEKKAYTLVLKGNMALERVKFPKGTTGFALDSLARQFLWAEGLDYRHGTGHGVGSFLNVHEGPIGIGTRVQYSEVSLAVGNVVSDEPGYYEDGKFGIRIENMIMVKEVETSHKFGDKPYLGFEHVTMTPHCRNLVDMSLLGEDEKQFINDYHKEVYEKTSGYFEDDALTLKWLKRETAPY
Enzyme Length 605
Uniprot Accession Number E5ABQ8
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 67,951
Kinetics
Metal Binding METAL 402; /note=Manganese 2; /evidence=ECO:0000250; METAL 413; /note=Manganese 1; /evidence=ECO:0000250; METAL 413; /note=Manganese 2; /evidence=ECO:0000250; METAL 511; /note=Manganese 1; /evidence=ECO:0000250; METAL 525; /note=Manganese 1; /evidence=ECO:0000250; METAL 525; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda