Detail Information for IndEnz0002018702
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;