| IED ID | IndEnz0002002339 |
| Enzyme Type ID | protease002339 |
| Protein Name |
Methionine aminopeptidase MAP MetAP EC 3.4.11.18 Peptidase M |
| Gene Name | map SAV1888 |
| Organism | Staphylococcus aureus (strain Mu50 / ATCC 700699) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain Mu50 / ATCC 700699) |
| Enzyme Sequence | MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDENFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQKVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAHVLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTKDGPILTTKIEEE |
| Enzyme Length | 252 |
| Uniprot Accession Number | P0A078 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 76; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; BINDING 175; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322" |
| 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_01974}; |
| 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_01974}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (10); Binding site (2); Chain (1); Helix (5); Metal binding (7) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1QXW; 1QXY; 1QXZ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,502 |
| Kinetics | |
| Metal Binding | METAL 93; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 104; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 104; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 168; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 202; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 233; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 233; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322" |
| Rhea ID | |
| Cross Reference Brenda |