2.3.1.193	[elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA	tRNAMet cytidine acetyltransferase acetylates the wobble base C34 of the elongation-specific tRNAMet. TmcA specifically recognizes the anticodon stem of tRNAMet, thus distinguishing between tRNAMet and tRNAIle2, which is structurally similar and has the same anticodon loop	Escherichia coli	[elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate + coenzyme A	-	?	407458	
2.3.1.193	[elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA	ATP/GTP hydrolysis by TmcA is stimulated in the presence of acetyl-CoA and tRNAMet. TmcA hydrolyses ATP or GTP between the beta- and gamma-phosphates, as shown by the detection of labelled ADP (or GDP). A mutation study reveals that Escherichia coli TmcA strictly discriminates elongator tRNAMet from the structurally similar tRNAIle by mainly recognizing the C27–G43 pair in the anticodon stem	Escherichia coli	[elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate + coenzyme A	-	?	407458	
2.3.1.193	[elongator tRNAMet]-cytidine34 + GTP + acetyl-CoA	-	Escherichia coli	[elongator tRNAMet]-N4-acetylcytidine34 + GDP + phosphate + coenzyme A	-	?	410653