IED ID | IndEnz0002002316 |
Enzyme Type ID | protease002316 |
Protein Name |
Methionine aminopeptidase MAP MetAP EC 3.4.11.18 Peptidase M |
Gene Name | map CA_C3111 |
Organism | Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium acetobutylicum Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
Enzyme Sequence | MIIIKNDTEIEYMRQAGKIVGETLNMLEKAAKPGVTTADLDRLAEDFIKKYNAIPSFKGYGGFPASICTSINEEVIHGIPSKHRVLHEGDIISVDCGAILNGYQGDAARTFAIGEISEEAAKLIKVTKESFFKGVEKAVIGNRLTDISHSIQEYVESFGYGVVRDYVGHGIGKEMHEDPEVPNYGRPGRGPKLVHGMVLAIEPMVDVGTYMVKTQSNDWTVVTQDGSLAAHYENTVAILDNGPEILTLCE |
Enzyme Length | 250 |
Uniprot Accession Number | P69000 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 77; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; BINDING 176; /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); Metal binding (7) |
Keywords | Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome |
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 | 27,301 |
Kinetics | |
Metal Binding | METAL 95; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 106; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 106; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 169; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 202; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 233; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 233; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974 |
Rhea ID | |
Cross Reference Brenda |