IED ID | IndEnz0002002264 |
Enzyme Type ID | protease002264 |
Protein Name |
Methionine aminopeptidase 1 MAP 1 MetAP 1 EC 3.4.11.18 Peptidase M |
Gene Name | map BSU01380 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MIICKTPRELGIMREAGRIVALTHEELKKHIKPGISTKELDQIAERFIKKQGAIPSFKGYNGFRGSICVSVNEELVHGIPGSRVLKDGDIISIDIGAKLNGYHGDSAWTYPVGNISDDDKKLLEVTEESLYKGLQEAKPGERLSNISHAIQTYVENEQFSVVREYVGHGVGQDLHEDPQIPHYGPPNKGPRLKPGMVLAIEPMVNAGSRYVKTLADNWTVVTVDGKKCAHFEHTIAITETGFDILTRV |
Enzyme Length | 248 |
Uniprot Accession Number | P19994 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 77; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; BINDING 175; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974 |
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, ECO:0000269|PubMed:16207374}; |
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, ECO:0000269|PubMed:16207374}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Metal binding (7) |
Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
Interact With | |
Induction | INDUCTION: Expression increases gradually during the log phase of growth. {ECO:0000269|PubMed:16207374}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16207374}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 27,409 |
Kinetics | |
Metal Binding | METAL 94; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 105; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 105; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 168; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 201; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 232; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 232; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974 |
Rhea ID | |
Cross Reference Brenda |