| IED ID | IndEnz0002002407 |
| Enzyme Type ID | protease002407 |
| Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
| Gene Name | BC1G_04189 |
| Organism | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | MAAQVTDALKNLKVKDPNAVVESAAEAKANGNAQPEAEAEDSDDDDEEPVNGEGAGEGGAKKKRKRKKKPKKKAGANPKVQSSPPRVLLSNLFPSGEYPVGEEVEYRDENNYRTTSEEKRYLDRMNNDFLQEYRQGAEIHRQVRQYAKANIKPGQTLTEIAEGIEDSVRALTGHPGLEEGDNIKGGVAFPTGVNLDHIAAHYSPNAGNKTVLAYENVMKVDFGVHINGRIVDSAFTIAFDPMYDNLLEAVKQATNTGIKEAGIDARLGEIGEHIQETMESYEVEIKGQTYQVKPIRNLNGHDILQWKIHGGKSVPIVKSNDQTKMEEGEVFAIETFGSTGNGYVRDDLECSHYAKVADAPNVPLRIASAGKLLNVINKNFGTLPFCRRYLDRLGQDKYLLGLNALVSHGIVQDYPPLVDKKGSYTAQFEHTIVLRPNCKEVISRGDDY |
| Enzyme Length | 448 |
| Uniprot Accession Number | A6RTU0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 201; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 309; /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 (2); Metal binding (7); Region (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease |
| 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 | 49,382 |
| Kinetics | |
| Metal Binding | METAL 221; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 232; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 232; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 301; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 334; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 429; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 429; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |