| IED ID | IndEnz0002002383 |
| Enzyme Type ID | protease002383 |
| Protein Name |
Methionine aminopeptidase 2-2 MAP 2-2 MetAP 2-2 EC 3.4.11.18 Peptidase M |
| Gene Name | AFUA_2G01750 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MGSKSPEGHRQAPHASNCNELKPANPDPQISQNGSGSADLDRGVIGDDDDDEDAEENGVNTETPNVGKLNQPPFPNLDQVHVTTTDGLCITEKKKKRKKSNKKKKKTKSGALPATELKQTSPPRVLVSTLFPSEYPVGELVPYDCTARTTDEELRYNSRLWDDDFLPDYRQAAEIHRQVRQYAQKELIKPGATLLSIAEGIEDGVRALSGHQGLEPGDFFKAGMGFPTGLCLNHIAAHWTPNPREKDVILDKGDVLKVDFGVHVNGRIVDSAFTVAFDDKYDNLLTAVREATNTGIKHAGVDARMSDIGAAIQEVMESYEVEIDGKVFPVKAIRNITGHDILRYHIHGGKQIPFIKNNNQDKMEEGEVYAIETFGSTGRGFLDDDVGVYGYGRNENMSGANLRLSSAKSLLKTIDASFGSIVFSRRYLERLGVKNYLLGMKNLIDNGIVECYSPLVDVKGSYTAQFEHTILLHSGGKEVISRGDDY |
| Enzyme Length | 486 |
| Uniprot Accession Number | Q4WII3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 238; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 347; /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 (4); 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 | 53,508 |
| Kinetics | |
| Metal Binding | METAL 259; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 270; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 270; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 339; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 372; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 467; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 467; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |