| IED ID | IndEnz0002002563 |
| Enzyme Type ID | protease002563 |
| Protein Name |
Methionine aminopeptidase MAP MetAP EC 3.4.11.18 Peptidase M |
| Gene Name | map TON_0362 |
| Organism | Thermococcus onnurineus (strain NA1) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Thermococcus Thermococcus onnurineus Thermococcus onnurineus (strain NA1) |
| Enzyme Sequence | MDEREALIKAGEIARQVKKEVISLIKPGTKLYDIAEFVERRIIELGGKPAFPCNLSINEIAAHYTPYKGDETVLKEGDYLKVDIGVHVDGYIADTALTFRVGMEEDDLVTAAREALENAIKVIRAGIKINEIGKAIEETIRGYGFNPIVNLSGHKIERYKLHAGISIPNIYRPADSYVLKEGDVIAIEPFATTGAGQVIEVPPALIFMYLRDRPVRMAQARRVLMHIKREYNGLPFAYRWLQGFMPEGQLKLALAQLDRVGAIYSYPILREVRGGLVAQFEHTVIVEKEGAYITT |
| Enzyme Length | 295 |
| Uniprot Accession Number | B6YTG0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 63; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; BINDING 162; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01975 |
| 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_01975, ECO:0000269|PubMed:16761197}; |
| 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). {ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:16761197}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80-90 degrees Celsius. {ECO:0000269|PubMed:16761197}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:16761197}; |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Hydrolase;Metal-binding;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,013 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.68 mM for L-Met-p-nitroanilide {ECO:0000269|PubMed:16761197}; Note=kcat is 168 min(-1) with L-Met-p-nitroanilide as substrate.; |
| Metal Binding | METAL 83; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; METAL 94; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; METAL 94; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; METAL 154; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; METAL 188; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; METAL 281; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; METAL 281; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01975 |
| Rhea ID | |
| Cross Reference Brenda |