Aminoalkylphosphonate N-acetyltransferase which is able to acetylate a range of aminoalkylphosphonic acids, including (S)-1-aminoethylphosphonate ((S)-1AEP) and 2-aminoethylphosphonate, using acetyl-CoA as acetyl donor. Its physiological role in S.typhimurium is unclear. However, by acetylating (S)-1AEP, PhnO would protect against the deleterious effects of (S)-1AEP, a structural analog of D-alanine that has antibacterial properties. acetyl-CoA + aminomethylphosphonate = 2-N-acetamidomethylphosphonate + CoA (S)-1-aminoethylphosphonate + acetyl-CoA = [(1S)-1-acetamidoethyl]phosphonate + CoA Requires a divalent metal ion for activity. In vitro, exhibits a preference for Ni(2+) followed by Mn(2+) and very poor activity with Mg(2+). However, it is unclear what the physiologically relevant metal ion is. kcat is 13.1 sec(-1) for the acetylation of (S)-1AEP. kcat is 14.7 sec(-1) for the propionylation of (S)-1AEP. kcat is 0.4 sec(-1) for the malonylation of (S)-1AEP. kcat is 7.0 sec(-1) for the acetylation of aminomethylphosphonate. kcat is 9.0 sec(-1) for the acetylation of 2-aminoethylphosphonate. kcat is 5.4 sec(-1) for the acetylation of 3-aminopropylphosphonate. kcat is 0.5 sec(-1) for the acetylation of 4-aminobutylphosphonate. kcat is 7.4 sec(-1) for the acetylation of 1-aminopropylphosphonate. kcat is 1.0 sec(-1) for the acetylation of 1-aminobutylphosphonate. kcat is 14.8 sec(-1) for the acetylation of 2-aminoethanesulfonate. kcat is 20 sec(-1) for the acetylation of 2-aminoethanesulfinate (in the presence of Ni(2+)). Homodimer. Reaction proceeds via an ordered, sequential kinetic mechanism with AcCoA binding first followed by aminoalkylphosphonate.