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). 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. Irreversibly inhibited by the fungal metabolite fumagillin and the fumagillin analog TNP470, antiangiogenic drugs. Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.