Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy

acetyl-CoA:N-terminal Met-Asn/Gln/Asp/Glu-[protein] Met-Nalpha-acetyltransferase

(1) acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein] + CoA;
(2) acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA;
(3) acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA;
(4) acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA

acetyl-CoA [CPD:C00024];
N-terminal L-methionyl-L-asparaginyl-[protein];
N-terminal L-methionyl-L-glutaminyl-[protein];
N-terminal L-methionyl-L-aspartyl-[protein];
N-terminal L-methionyl-L-glutamyl-[protein]

N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.

EC 2.3.1.254 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.254