| IED ID | IndEnz0002002276 |
| Enzyme Type ID | protease002276 |
| Protein Name |
Methionine aminopeptidase 1D, mitochondrial MAP 1D MetAP 1D EC 3.4.11.18 Methionyl aminopeptidase type 1D, mitochondrial Peptidase M 1D |
| Gene Name | Metap1d Map1d Metapl1 Mnpepl |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAAPIGVPLLVRGGCQRILSSPLNHIYLHKRSGSQQRRHFFFWRQRDISHSVVSPAAVSPAHPVPKRIKKPDYVTTGIVPDWGDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISRITHQNGLQVCPHFVGHGIGSYFHGHPEIWHHANDNDLPMEEGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITPRGVEILTKLPQEA |
| Enzyme Length | 335 |
| Uniprot Accession Number | Q9CPW9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 161; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 259; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03174}; |
| DNA Binding | |
| EC Number | 3.4.11.18 |
| Enzyme Function | FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-Rule:MF_03174}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Binding site (2); Chain (1); Metal binding (7); Sequence conflict (1); Transit peptide (1) |
| Keywords | Alternative splicing;Aminopeptidase;Hydrolase;Metal-binding;Mitochondrion;Protease;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03174}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12520002; 14610273; 16934000; 18614015; 18799693; 21267068; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,262 |
| Kinetics | |
| Metal Binding | METAL 178; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 189; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 189; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 252; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 284; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 315; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 315; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| Rhea ID | |
| Cross Reference Brenda |