| IED ID | IndEnz0002002366 |
| Enzyme Type ID | protease002366 |
| Protein Name |
Methionine aminopeptidase 2-1 MAP 2-1 MetAP 2-1 EC 3.4.11.18 Peptidase M |
| Gene Name | Lema_P106830 |
| Organism | Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Leptosphaeriaceae Leptosphaeria Leptosphaeria maculans species complex Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) Leptosphaeria maculans 'brassicae' group Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam) |
| Enzyme Sequence | MGSKSPNGEDRGPNGPSAKKAVASINPPKSAAASGLLRGALEDQDEDGDDDEGKIGADMNVSEKTANGTKKRRRNNKKKKSAQAAQQTAPPRVEIATLFHNRPYPEGEIVEYGINDENLVRTTDEEFRHLAVANNMNDEFLRDYRKAAEVHRQVRQYAQTIAKPGISMTELAREIEDGVRALVGHQGIETGDSLKAGMGFPTGLCINNVAAHWTPNPGAREVVLQHDDVLSIDFGVHVNGRIVDSAFTVAFNPMYDKLLTAVKAATNTGLKESGIDARMDYISETIQEVMESYEVMINGKPLPVKALSSLSGHNILRYKIHGDKQVPFVKTRTSQRMEEGDVFAIETFGSTGIGRTRDDVGVYGYSRNENVSTAGVHLASAKSLLKAIDENFGTLPFSRNYLERIGVKNYHLGMRSLIASGVVECYAPLVDTPGSYVAQFEHTVLLRPNCKEIISRGDDY |
| Enzyme Length | 460 |
| Uniprot Accession Number | E4ZYY3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 212; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 321; /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); 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 | 50,338 |
| Kinetics | |
| Metal Binding | METAL 233; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 244; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 244; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 313; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 346; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 441; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 441; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |