| IED ID | IndEnz0002002314 |
| Enzyme Type ID | protease002314 |
| Protein Name |
Methionine aminopeptidase MAP MetAP EC 3.4.11.18 Peptidase M |
| Gene Name | map CPn_1009 CP_0844 CpB1046 |
| Organism | Chlamydia pneumoniae (Chlamydophila pneumoniae) |
| Taxonomic Lineage | cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia pneumoniae (Chlamydophila pneumoniae) |
| Enzyme Sequence | MKRNDPCWCGSGRKWKQCHYPQPPKMSPEALKQHYASQYNILLKTPEQKAKIYNACQITARILDELCKASQKGVTTNELDELSQELHKKYDAIAAPFHYGSPPFPKTICTSLNEVICHGIPNDIPLKDGDIMNIDVSCIVDGYYGDCSRMVMIGEVPEIKKKICQAALECLNDSIAILKPGIPLCEIGEAIEARADTYGFSVVDQFVGHGVGIEFHENPYVPHYRNRSMIPLAPGMIFTIEPMINVGKKEGVVDPKNQWEARTCDNQPSAQWEHTIAITETGYEILTLLND |
| Enzyme Length | 291 |
| Uniprot Accession Number | Q9Z6Q0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 118; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; BINDING 216; /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}; |
| 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 | Binding site (2); Chain (1); Erroneous initiation (2); 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 | 32,596 |
| Kinetics | |
| Metal Binding | METAL 135; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 146; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 146; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 209; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 241; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 273; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 273; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974 |
| Rhea ID | |
| Cross Reference Brenda |