| IED ID | IndEnz0002002358 |
| Enzyme Type ID | protease002358 |
| Protein Name |
Methionine aminopeptidase 2-1 MAP 2-1 MetAP 2-1 EC 3.4.11.18 Peptidase M |
| Gene Name | af410 AFUA_8G00410 |
| 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 | MTVDAPELLEKLRITDAGANGADMSSSTSAAANGTGKEVDDGSDDDGTENPPAVAAEHSTAKKKKNKKRKPKKKQPKVQTDPPSIPLSQLFPNNSYPKGEEVEYKDENRYRTTSEEKRHLDNLNSDFLSDYRQAAEAHRQVRQWAQRNIKPGQTLLEIANGIEESARCLVGHDGLTEGDSLIAGMGFPTGLNIDNIVAHYSPNAGCKTVLAQNNVLKVDIGIHVGGRIVDSAFTMAFDPMYDNLLAAVKDATNTGVREAGIDVRVGELGGYIQEAMESYECEIRGKTYPIKAIRNLCGHTILPYSIHGTKNVPFVKSNDMTKMEEGDVFAIETFGSTGSGRYVEGGEVSHYALRGDADRKDLTLSSARSLLTAIKKNFSTIPFCRRYLDRIGQEKYLLGLNYLVKSGIVEDYPPLNEKPGTYTAQFEHTILLRPTVKEVISRGDDY |
| Enzyme Length | 446 |
| Uniprot Accession Number | Q4WAY7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 199; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 307; /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) (By similarity). Part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24082142, PubMed:24568283). Since fumagillin is known to inhibit eukaryotic type 2 methionine aminopeptidase, af410 encodes a self-resistant enzyme for A.fumigatus toward fumagillin (PubMed:23488861). {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:23488861, ECO:0000269|PubMed:24082142, ECO:0000269|PubMed:24568283}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Compositional bias (4); Erroneous gene model prediction (1); Metal binding (7); Region (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Expression is controlled by the fumagillin biosynthesis cluster regulator fumR (PubMed:24082142). Expression is also under the control of the developmental and secondary metabolism regulator veA (PubMed:24116213). {ECO:0000269|PubMed:24082142, ECO:0000269|PubMed:24116213}. |
| 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 | 48,996 |
| Kinetics | |
| Metal Binding | METAL 219; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 230; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 230; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 299; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 332; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 427; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 427; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |