IED ID | IndEnz0002002406 |
Enzyme Type ID | protease002406 |
Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
Gene Name | AO090120000238 |
Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
Enzyme Sequence | MGSKTFEGEGQRGGNDPSNSTSPNSAGGEPRGAHLSRDGDGSLGDGDGDDGADGDEKDGAVTTTPLTEQQPSSETTSKKKKRRKPKKKISALKQSSPPRVPLDDLFPTGQFPVGETHEYGSVVEGTARTTSEEVRYLSRNYLQDDSVLTDYRKAAEIHRQVRHWTQENVRPGQTLTEIAVGIEDGVRALLDNAGLETGQCLQSGMGFPTGLALNDCVAHYTPNPGQKDIVLQASDVMKVDFGVHINGWIVDSAFTMSFDPTYDNLLAAVKDATNTGIKNAGIDVRISDVSAAIQEAMESYEVEIGGKVFPVKPVRDISGHNINRYQIHGGKSIPFVKNSSQTKMEEGEIFAIETFGSTGRGSTVEGFGVYGYGKDPNAPKKVSSPLASARSLYKTINENFGSIVFCRRYLERLGVERYLAGMNSLVNNGIVEQYAPLMDMKGSYSAQFEHTILLRESCKEVVSRGNDY |
Enzyme Length | 468 |
Uniprot Accession Number | Q2U6H2 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 219; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 328; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
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_03175}; |
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_03175}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Compositional bias (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_03175}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 50,724 |
Kinetics | |
Metal Binding | METAL 240; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 251; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 251; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 320; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 353; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 449; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 449; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Rhea ID | |
Cross Reference Brenda |