Figure 4.

Sequence alignment of ValA with representative related enzymes. The sequence of ValA is listed first, and its secondary structure elements are schematically shown above the sequence. Other sequences in descending order are AvDDGS (A. variabilis DDGS, Ava_3858), AmEVS (Ac. mirum EVS, Amir_2000), PDB entry 1DQS (As. nidulans DHQS), PDB entry 2D2X (B. circulans DOIS), and PDB entry 1JQ5 (B. stearothermophilus glycerol dehydrogenase). For the structurally known proteins, the residues in β-strands (yellow), α-helices (teal), 3₁₀-helices (blue), and π-helices (orange) are highlighted. Residues involved in metal binding (m), NAD⁺ binding (n), and substrate binding and/or catalysis (∗) are denoted below the sequences, and active site residues with notable variation (↓) are denoted above the sequences.