| IED ID | IndEnz0002012599 |
| Enzyme Type ID | protease012599 |
| Protein Name |
Xaa-Pro aminopeptidase 3 X-Pro aminopeptidase 3 EC 3.4.11.9 Aminopeptidase P3 APP3 |
| Gene Name | xpnpep3 DDB_G0282075 |
| Organism | Dictyostelium discoideum (Slime mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Dictyostelia (dictyostelid cellular slime molds) Dictyosteliales Dictyosteliaceae Dictyostelium Dictyostelium discoideum (Slime mold) |
| Enzyme Sequence | MNNICKLNKFIISKSSSSLSSTSSKIKTNCLIKNAKMFSSSLNLNRFYSTNNTNNNKLKKPLSIGQATFETHPYLLDKNEITKGIKMKEFKDRREKLMKNFPIGSVVVIFTPPEPMMSYDIPWSFRQNTNFNYLTGFNEPEAVLVLVKTSELDHQSYLFVRERNEEKEKWDGARCGGENVKKYFGIDFGYNLTNRDIPILGKLLKSTTDGKLYCNTTPWNQLSNKLEPFLENIKFYTVESLLQQIRLIKSDAEIKMMLKSGEIAGTSFHETMKYTGTKSSSSSSSSSSSPLNEYQVSAYFEWCVKDKGAQRMSYPPVVAGGDNGHTLHYIQNNQLLNYCDLLLMDAGCEYWGYTSDITRTFPVSGKFTEAQSEVYQAVLDVNKKCIELCKPGETINSIHLKSVELIQAHLKRLGIINESNPNDYRLYYPHSIGHYLGMDTHDTLDFDYGVTLEPGMIITIEPGIYISKYDSNVPEKYRGISIRVEDDVVIPNLNNSPLVLTHLAPKEISEIESIMSNK |
| Enzyme Length | 518 |
| Uniprot Accession Number | Q54T46 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 314; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7; BINDING 345; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7; BINDING 356; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7; BINDING 434; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7; BINDING 441; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7; BINDING 461; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7; BINDING 485; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9NQH7 |
| 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; Evidence={ECO:0000250|UniProtKB:Q9NQH7}; |
| 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, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. {ECO:0000250|UniProtKB:Q9NQH7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (7); Chain (1); Metal binding (7); Transit peptide (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NQH7}. Cytoplasm {ECO:0000250|UniProtKB:Q9NQH7}. Note=Mainly mitochondrial. {ECO:0000250|UniProtKB:Q9NQH7}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,869 |
| Kinetics | |
| Metal Binding | METAL 345; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQH7; METAL 356; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQH7; METAL 356; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQH7; METAL 434; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQH7; METAL 461; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQH7; METAL 485; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQH7; METAL 485; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQH7 |
| Rhea ID | |
| Cross Reference Brenda |