IED ID | IndEnz0002002266 |
Enzyme Type ID | protease002266 |
Protein Name |
Methionine aminopeptidase 1 MAP 1 MetAP 1 EC 3.4.11.18 Peptidase M 1 |
Gene Name | metap1 DDB_G0279433 |
Organism | Dictyostelium discoideum (Slime mold) |
Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Dictyostelia (dictyostelid cellular slime molds) Dictyosteliales Dictyosteliaceae Dictyostelium Dictyostelium discoideum (Slime mold) |
Enzyme Sequence | MEGILCASPGCGKPAKLQCPTCVNLKLETPSHFCSQECFKTFWPLHKMYHQKGQPENLPSQFRNYKFTGPLRPTNITPMRKAPEGIELPDYAIGSIPISERVADRKNMANIIHTPEEIEIMRQLGKMSREVLDIAGNAAKVGMTTEELDIIVHNAVIERGAYPSPLNYYKFPKSCCTSLNEVICHGIPDERPLRDGDILNVDVTLYWKGFHSDLNETYLIGNVDERGKNLVKCAYDCLELAVAMCKPGTLYRELGDAIQKHANKQGFSVVKNFCGHGIGRLFHCNPTVPHYSKNKAVGAMKVGHVFTIEPMINEGTWQDEIWPDSWTAVTADGKRSAQFEHTLVITETGCEVLTKRTNGSYIDRHFK |
Enzyme Length | 367 |
Uniprot Accession Number | Q54WU3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 185; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 283; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
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_03174}; |
DNA Binding | |
EC Number | 3.4.11.18 |
Enzyme Function | FUNCTION: Cotranslationally 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_03174}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Metal binding (7); Region (1) |
Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 41,185 |
Kinetics | |
Metal Binding | METAL 202; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 213; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 213; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 276; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 309; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 340; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 340; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
Rhea ID | |
Cross Reference Brenda |