| IED ID | IndEnz0002002273 |
| Enzyme Type ID | protease002273 |
| 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 zgc:110461 |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MAAPCAAQCLYRTGGLRLLQRISRLPHCHKDASLAHQCQFHRSFFWRKPKTSHSVVRPAIVRPAYPVPKHIQRPDYVSSSKVPEWPDYIEIKDEEQIQGLRRACQLARHILLLTGNSLKVGMTTDEIDFIVHQEAIRHNGYPSPLHYGGFPKSVCTSVNNVVCHGIPDSRPLQDGDIINIDVTVYLEGYHGDTSETFLIGSVNDQGRKLVDVARQCRDQAIAACGPGQPLCVIGNIISNIANSNGFRVCPYFIGHGIGEYFHGHPEIWHHANDNDLKMEEGMSFTIEPILMEGTSGFRILSDKWTAVSVDDKRSAQFEHTVVITSDGVEILTKLPEED |
| Enzyme Length | 338 |
| Uniprot Accession Number | Q4VBS4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 164; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 262; /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 | Binding site (2); Chain (1); Metal binding (7); 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}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,785 |
| Kinetics | |
| Metal Binding | METAL 181; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 192; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 192; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 255; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 287; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 318; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 318; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| Rhea ID | |
| Cross Reference Brenda |