Figure 1

Multiple sequence alignment of the C-terminal segments of plant GADs. Multiple sequence alignment was created with Clustal W [15] and edited manually. The C-terminal CaMBDs of Petunia hybrida (PhGAD) [16], Arabidopsis thaliana (AtGAD1) [18] and Oryza sativa (OsGAD1) [5] have been characterized experimentally. Two conserved positively charged clusters of lysines that flank the CaMBD are marked with black lines [9]. The conserved tryptophan residue involved in CaM binding [16, 17], marked with an asterisk, is not present in OsGAD2, which does not bind CaM [5]. Rice GAD numbering is taken from Akama and Takaiwa [5]: OsGAD1 (AB056060, LOC_Os08g36320.1); OsGAD2 (AB056061, LOC_Os04g37500.1). Identical residues are shown with a black background, and similar residues are shown with a grey background. All enzymes were identified as belonging to the aspartate aminotransferase superfamily (fold type I) of PLP-dependent enzymes by the NCBI CD-Search tool [18].