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

acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nalpha-acetyltransferase

(1) acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA;
(2) acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA;
(3) acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA;
(4) acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA;
(5) acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA;
(6) acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA

acetyl-CoA [CPD:C00024];
N-terminal-glycyl-[protein] [CPD:C02038];
N-terminal-L-alanyl-[protein];
N-terminal-L-seryl-[protein];
N-terminal-L-valyl-[protein];
N-terminal-L-cysteinyl-[protein];
N-terminal-L-threonyl-[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. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.

EC 2.3.1.255 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.255