IED ID | IndEnz0002018788 |
Enzyme Type ID | protease018788 |
Protein Name |
Probable Xaa-Pro aminopeptidase P AMPP Aminopeptidase P EC 3.4.11.9 Aminoacylproline aminopeptidase Prolidase |
Gene Name | ampp NFIA_079250 |
Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
Enzyme Sequence | MLGFRSPIRLCKLSALGSAPLLPISRPKLFSTAVARYAADMETVNTTERLARLRQLMQEHKVDVYIVPSEDSHQSEYIAPCDGRREFISGFSGSAGTAIVSMTKAALSTDGRYFNQASKQLDSNWELLKRGVENVPTWQEWTTEQAEGGKVVGVDPSLITASGARSLEETLKRNGSSLVGISQNLVDLVWGKDRPAPPREKVRVHPDKFAGKTFQEKIADLRKELEKKKTAGFVISMLDEIAWLFNLRGSDIPYNPVFFAYAIITPTKAELYIDDDKITPEVVAHLGQDVVIKPYNSIFADAKALSEARKQEAGETASKFLLSNKASWALSLSLGGEEHVEETRSPIADAKAIKNEVELAGMRACHIRDGAALIEYFAWLENELVNKKTVLDEVDAADKLERIRTKHDLFAGLSFDTISSTGPNGAVIHYKPEKGTCSIIDPDAIYLCDSGAQYLDGTTDVTRTFHFGKPTELEKKAFTLVLKGLIAIDTAVFPKGTSGFALDALARQYLWKEGLDYLHGTGHGIGSYLNVHEGPIGIGTRVQYTEVPIAPGNVISDEPGFYEDGKFGIRIENVIMAREVQTTHKFGDKPWLGFEHVTMAPIGRNLIQPSLLSDLELKWVNDYHAEVWDKTHHFFENDEFTRSWLQRETAPITK |
Enzyme Length | 654 |
Uniprot Accession Number | A1DF27 |
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 | 72,591 |
Kinetics | |
Metal Binding | METAL 449; /note=Manganese 2; /evidence=ECO:0000250; METAL 460; /note=Manganese 1; /evidence=ECO:0000250; METAL 460; /note=Manganese 2; /evidence=ECO:0000250; METAL 558; /note=Manganese 1; /evidence=ECO:0000250; METAL 572; /note=Manganese 1; /evidence=ECO:0000250; METAL 572; /note=Manganese 2; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |