IED ID | IndEnz0002002400 |
Enzyme Type ID | protease002400 |
Protein Name |
Methionine aminopeptidase 2-3 MAP 2-3 MetAP 2-3 EC 3.4.11.18 Peptidase M |
Gene Name | NFIA_093940 |
Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
Enzyme Sequence | MTIDAPELLEKLKISDADANGADIPGSTSAAANGMLKEDDDSDDDVAENTPAVAAENGTAKKKKNKKRKPKKKQPKVQTDPPSIPLSQLFPNNTYPKGEEVEYKDENRYRTTSEEKRHLDNLNSDFLSDYRQAAEAHRQVRQWAQRNIKPGQTLLEIANGIEDSARRLVGHDGLTEGDSLIAGMGFPTGLNIDNIVAHYSPNAGCKTVLAQNNVLKVDIGIHVGGRIVDSAFTMAFDPMYDNLLAAVKDATNTGVREAGIDVRVGELGGYIQEAMESYECEINGKTHPIKAIRNLCGHTILPYSIHGTKSVPFIKSNDMTKMEEGDVFAIETFGSTGSGRYVEGGEVSHYALRGDANRKDLTLSSARSLLTAIKKNFSTIPFCRRYLDRIGQEKYLLGLNYLVKSGIVEDYPPLNEKQGTYTAQFEHTILLRPTVKEVISRGDDY |
Enzyme Length | 445 |
Uniprot Accession Number | A1DA84 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 198; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 306; /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;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 | 48,998 |
Kinetics | |
Metal Binding | METAL 218; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 229; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 229; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 298; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 331; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 426; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 426; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Rhea ID | |
Cross Reference Brenda |