| IED ID | IndEnz0002002389 |
| Enzyme Type ID | protease002389 |
| Protein Name |
Methionine aminopeptidase 2-2 MAP 2-2 MetAP 2-2 EC 3.4.11.18 Peptidase M |
| Gene Name | AN0369 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MGSKTPERDGHKGQENTTGPVECPLGGMPRGMHLATDGDGTIGDSGDDDDGEAHSTALINANANGNQKKKRKSKKKGKKKAAKQSSPPRVPLSQLFLQGKYPIGEVQEYQPNVENTSRTTAEEVRYKSRSHLEDDSFLNDYRKAAEVHRQVRKWTQERVKPGQGLMEIAEDIDDGVRALLGHAGLEPGDSLKAGLGFPTGLSLNNVVAHYTPNPGQKDIILQSSDVMKVDFGVHINGWIVDSAFTMTFDPVYDNLLAAVKDATNAGLKTAGIDVRISDVSAAIQEAMESYEVEIGGKTFPVKAVRNITGHNIKHYQIHGGKSVPFVKNSDQTKMEEGEIFAIETFGSTGRGYIYDDVGVYGYGKSYDAPRQVSLPLASARSLYKTINENFGTIVFCRRYLDRLGLQRYLAGMNTLVQHGVVDVYAPLVDIKGSYSAQFEHTVLLRESNKEVISRGDDY |
| Enzyme Length | 458 |
| Uniprot Accession Number | Q5BGG1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 209; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 318; /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); Erroneous gene model prediction (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 | 50,186 |
| Kinetics | |
| Metal Binding | METAL 230; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 241; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 241; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 310; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 343; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 439; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 439; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |