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). Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. 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). Fumagillin and its derivatives have been intensely studied for their potential use in the treatment of amebiasis, microsporidiosis and rheumatoid arthritis (PubMed:14913169, PubMed:12075057, PubMed:18209961). They have also interesting antiangiogenic properties by the irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:9177176). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.