| IED ID | IndEnz0002002275 |
| Enzyme Type ID | protease002275 |
| 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 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAAPSGVHLLVRRGSHRIFSSPLNHIYLHKQSSSQQRRNFFFRRQRDISHSIVLPAAVSSAHPVPKHIKKPDYVTTGIVPDWGDSIEVKNEDQIQGLHQACQLARHVLLLAGKSLKVDMTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLPMEEGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHEA |
| Enzyme Length | 335 |
| Uniprot Accession Number | Q6UB28 |
| 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 (By similarity). May play a role in colon tumorigenesis. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16568094}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:17929833}; |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Erroneous initiation (1); Metal binding (7); Natural variant (1); Transit peptide (1) |
| Keywords | Aminopeptidase;Hydrolase;Metal-binding;Mitochondrion;Protease;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:14532271}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19913121; 20379614; 20628086; 20877624; 26496610; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,088 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=573 uM for Met-pro-p-nitroanilide (at pH 8) {ECO:0000269|PubMed:17929833}; |
| 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 | 3.4.11.18; |