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Sequence alignments and substrate accommodations of the concerned residues. (A) Amino acid sequence alignments of KGUK from C. necator (1.) and 2-keto-3-deoxy-d-gluconate kinase (KDGK) from Thermus thermophilus (2.). Grey-shaded amino acids have been identified as active site residues in the crystallographic structure of the KDGK enzyme. Only three residues (shaded in black) are different in the C. necator enzyme. (B) Structure of the active site of KDGK from T. thermophilus.
