| IED ID | IndEnz0002002367 |
| Enzyme Type ID | protease002367 |
| Protein Name |
Methionine aminopeptidase 2-1 MAP 2-1 MetAP 2-1 EC 3.4.11.18 Peptidase M |
| Gene Name | NFIA_109310 |
| 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 | MAAQVTEKLQDLHLNGQNGDAKANSTAVGQTEAGEAEDDSDDEKEDGNAAPEAGAGGAAKKKKRKSKKKKKGGAKVQSSPPRVPVSNLFPNNQYPEGEIVEYKNENSYRTTNEEKRYLDRMNNDFLQEYRQAAEVHRQVRQYAQRTIKPGQTLTEIAEGIEDAVRALTGHQGLEEGDNLKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAHINGRIVDSAFTMTFDPVYDPLLEAVKDATNTGIREAGIDVRMSDIGAAIQEAMESYEVELNGTMYPVKCIRNLNGHNIDQHIIHGGKSVPIVKGSDQTKMEEGETFAIETFGSTGKGYVREDMETSHYALIPDAPSVPLRLSSAKNLLNVINKNFGTLPFCRRYLDRLGQEKYLLGLNNLVSSGIVQDYPPLCDVKGSYTAQFEHTILLRPTVKEVISRGDDY |
| Enzyme Length | 444 |
| Uniprot Accession Number | A1CXT5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 197; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 305; /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 | 48,772 |
| Kinetics | |
| Metal Binding | METAL 217; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 228; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 228; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 297; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 330; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 425; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 425; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |