2.1.1.229	FAD	required for oxidative cleavage of carboxymethyl group from cmnm5U34, FAD-binding site structure, overview	
2.1.1.229	S-adenosyl-L-methionine	-	
2.1.1.229	S-adenosyl-L-methionine	binding site structure, overview	
2.1.1.229	S-adenosyl-L-methionine	dependent on, the N-terminal MnmC2 domain is composed of residues 1-245 and contains the SAM binding site. The binding pocket is composed of mostly hydrophobic residues, except for Glu101 and Asp178	
2.1.1.229	S-adenosyl-S-carboxymethyl-L-homocysteine	i.e. [(3S)-3-amino-3-carboxypropyl]{[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}(carboxymethyl)sulfanium, the enzyme contains a cofactor, S-adenosyl-S-carboxymethyl-L-homocysteine (SCM-SAH), in which the donor methyl group is substituted by a carboxymethyl group. The carboxyl moiety forms a salt-bridge interaction with Arg199 that is conserved in a large group of CmoA-related proteins but is not conserved in other S-adenosyl-L-methionine-containing enzymes. The active site contains one molecule cofactor S-adenosyl-S-carboxymethyl-L-homocysteine per monomer, and not S-adenosyl-L-methionine