| IED ID | IndEnz0002013649 |
| Enzyme Type ID | protease013649 |
| Protein Name |
Xaa-Pro aminopeptidase 1 EC 3.4.11.9 Aminoacylproline aminopeptidase Cytosolic aminopeptidase P Soluble aminopeptidase P sAmp X-Pro aminopeptidase 1 X-prolyl aminopeptidase 1, soluble |
| Gene Name | xpnpep1 xpnpepl xpnpepl1 DDB_G0290501 |
| 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 | MQRVLNKIISKDTINTMGKVAISKKVEKLRTFMKDQSLSAYIVPSEDAHQSEYICVKDKRREYISGFSGSAGCVVITLDNQLLWTDGRYWLQAEKELESNWKIMKDRVVGEPTIQDWLLSNLNKENKVGIDSRLISKGYYDSMKLVLKEKSIDIKFDEDGENLIDKVRESFKDEEEIPEYPKNSIFFLEDKFTGKQSNEKLKEIREEMKKQSADLMVVSALDEIAWLLNLRGSDISFNPVFLSYVVVEHEKVTLFVDESKLNDKTKSQLPSGIAISPYSSVFEYLRNSDKQGKKIWIDPRSSVALYNCVSISNLLEKINPILLSKAIKNETEIQGMKNAHIRDAVALIQFLAWMEEEIVEKSDETSHTEYSVCEKLEGFRRQQTDFVSLSFDTISSINANGAIIHYKPDETTSATIVKGMYLVDSGAQYLDGTTDVTRTLHYGKPTQHEIDCYTRVLRGHVGLSLLKFPNRVNGRDIDCVARTHLWSVGLDYAHGTGHGVGSFLNVHEGPQGISYRAIANPTNLQAGMTLTNEPGYYESGNFGIRIENVMIVAPVTTQFNNGKFIGFDNITLVPYERKLINLEMLTKDEINFINDYYKEIGEKILPLIEKTNNQKSINWLKNQIKPL |
| Enzyme Length | 627 |
| Uniprot Accession Number | Q54G06 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 88; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 405; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 498; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 507; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 533; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750 |
| 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, such as Arg-Pro-Pro. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (5); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,393 |
| Kinetics | |
| Metal Binding | METAL 424; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 435; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 435; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 498; /note=Manganese 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 533; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 547; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 547; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7 |
| Rhea ID | |
| Cross Reference Brenda |