| IED ID | IndEnz0002018702 |
| Enzyme Type ID | protease018702 |
| Protein Name |
Aspartyl aminopeptidase 1 EC 3.4.11.21 |
| Gene Name | aap1 SPAC4F10.02 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MTATAKSCALDFLDFVNASPTPYHAVQNLAEHYMSHGFQYLSEKSDWQSKIEPGNSYFVTRNKSSIIAFSIGKKWKPGNGFSIIATHTDSPTLRLKPKSQKSAYGYLQVGVEKYGGGIWHTWFDRDLSLAGRVMVEEEDGRVIQYNVHIDRPLLRIPTLAIHLDPSANSSFSFNMETEFVPLIGLENELAKEETSDNGDKYHHPVLLSLLANEISKSLETTIDPSKIVDFELILGDAEKARLGGIHEEFVFSPRLDNLGMTFCASQALTKSLENNSLDNESCVRVVPSFDHEEIGSVSAQGAESTFLPAVLQRICELGKESSLFSISMVKSFLVSADMAHAMHPNYSSRYENSNTPFLNKGTVIKVNANQRYTTNSAGIVLLKKVAQLADVPIQSFVVRNDSPCGSTIGPKLAAMTGMRTLDLGNPMLSMHSCREMCGSKDFEYAVVLFSSFFQNFANLEEKIIIDE |
| Enzyme Length | 467 |
| Uniprot Accession Number | O36014 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 162; /note=Substrate; /evidence=ECO:0000250; BINDING 292; /note=Substrate; /evidence=ECO:0000250; BINDING 337; /note=Substrate; /evidence=ECO:0000250; BINDING 340; /note=Substrate; /evidence=ECO:0000250; BINDING 365; /note=Substrate; /evidence=ECO:0000250; BINDING 372; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.; EC=3.4.11.21; Evidence={ECO:0000269|PubMed:20044953}; |
| DNA Binding | |
| EC Number | 3.4.11.21 |
| Enzyme Function | FUNCTION: Aspartyl aminopeptidase that is able to remove aspartyl residue at N-terminus of angiotensin I. Acts also as a chaperone and efficiently suppressed the thermal aggregation of citrate synthase. {ECO:0000269|PubMed:20044953}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Metal binding (6); Sequence conflict (2) |
| Keywords | 3D-structure;Aminopeptidase;Chaperone;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1) |
| Cross Reference PDB | 7DDE; |
| Mapped Pubmed ID | 16802154; 20473289; 21760946; 23697806; 28410370; 28945192; 33260998; 34169534; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,741 |
| Kinetics | |
| Metal Binding | METAL 87; /note=Zinc 1; /evidence=ECO:0000250; METAL 256; /note=Zinc 1; /evidence=ECO:0000250; METAL 256; /note=Zinc 2; /evidence=ECO:0000250; METAL 293; /note=Zinc 2; /evidence=ECO:0000250; METAL 337; /note=Zinc 1; /evidence=ECO:0000250; METAL 431; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.21; |