Figure 2 | Scientific Reports

Figure 2

From: A novel allele of L-galactono-1,4-lactone dehydrogenase is associated with enhanced drought tolerance through affecting stomatal aperture in common wheat

Figure 2

Multiple alignment of the deduced amino acid sequences of TaGLDH-A1, -B1 and -D1 homoeologs and orthologous GLDH proteins from Arabidopsis (AtGLDH), cauliflower (BoGLDH), sweet potato (IbGLDH) and tobacco (NtGLDH).

Arrow indicates the likely cleavage site of the mitochondrial targeting peptide. The underlined sequence element is required for FAD binding. The conserved cysteine residue labeled in purple is involved in regulating the enzyme activity of plant GLDH proteins, whereas the E-R pair of residues marked in blue are required for efficient substrate binding and catalysis. The glutamic acid (E) marked in red is deleted in a novel allele (TaGLDH-A1b) of TaGLDH-A1. Asterisks denote residues conserved among the compared GLDHs. The UniProtKB numbers for AtGLDH, BoGLDH, IbGLDH and NtGLDH are Q8GY16, O47881, Q9ZWJ1 and Q9FXL9, respectively.

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