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. 2014 Mar;196(5):1064–1072. doi: 10.1128/JB.01308-13

FIG 3.

FIG 3

Sequence alignment of DadD from M. jannaschii with homologs from other methanogens, as well as with previously characterized enzymes. The residues are highlighted in the following way: a cyan background with black lettering indicates residues coordinating the metal, a blue background with white letters indicates residues interacting with the ribose moiety of the substrate, a pink background with black letters indicates residues interacting with the purine base, a purple background with white letters indicates residues involved in forming a hydrophobic pocket to bind the 5′-methylthio moiety of MTA, a gray background with black letters indicates residues interacting with the 5′-methylthio moiety of MTA, and the arginines residues interacting with the SAH carboxylate are highlighted by a green background with black letters and are underlined. M. jannaschii numbering is used.