Fig. 7
Amino acid alignments of Family A PFKs including both ATP-PFKs and PPi-PFKs, that have been purified and characterized to phosphorylate sugar phosphates with various phosphate donors. Protein crystal structures have been solved for E. coli PfkA, G. stearothermophilus PfkA and B. burgdorferi Pfp which aided in identifying residues implicated in binding F6P (F), ATP (A), PPi (P) and effectors (E). The secondary structures displayed above the alignment was based off the secondary structures determined from the crystal structure of G. stearothermophilus PfkA, thus similar folds should be present in the highly conserved region of the other PFKs. The percent similarity between C. thermocellum PfkA and each of the other PFKs were placed at the end of the alignment, while percent similarity compared to C. thermocellum Pfp was placed in parentheses. 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. Note that the PfkA sequences were truncated to focus on the N-terminal which contains the binding domains, whereas majority of the Pfp sequence was used during alignment. The amino acid numbering in the alignment corresponds to E. coli PfkA