Fig. 10

Amino acid alignments of Family B PFKs including the characterized ATP/GTP PfkB from C. thermocellum; along with the characterized PfkBs from a diverse group of microorganisms, which have been shown to utilize many different substrates. Protein crystal structures have been solved for E. coli ribokinase (E. coli_Rb), which was used as a template to identify residues that directly hydrogen bond with ribose (R) and ATP (A), while indirect hydrogen bonds via water molecule with ribose (r) and ATP (a) was also shown. Residues from the protein that make van der Waals contacts with ribose (W) and ATP (w). The protein crystal structure of E. coli PFK-2(E. coli_PFK) was used to identify residues interacting with monovalent (M) and divalent cation (D). The percent similarity between C. thermocellum PfkB and each of the other PfkB were placed at the end of the alignment. Segments highlighted in red, identical residues, while letters in red represent similar residues. The sequences were aligned with MAFFT and the figure prepared with ESPript. The residues making up each of the PfkB single domain were used in the alignment