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Figure 2 | Biology Direct

Figure 2

From: A computational analysis of the three isoforms of glutamate dehydrogenase reveals structural features of the isoform EC 1.4.1.4 supporting a key role in ammonium assimilation by plants

Figure 2

The two dinucleotide-binding motifs of plant GDH4. The part of each consensus sequence corresponding to the central domain of GDHs was extracted using the full consensus sequence of subset I3 as the template. The 15 subsets (J to L) are presented in five groups (1 to 5) according to the percentages of identity. Secondary structures indicated above the alignment were generated using the bovine GDH3 complexed with NADPH and glutamate (PDB # 1HWZ) as the template. Amino acid position indicated above the alignments is that of plant GDH4 (Ref). Plain vertical boxes. amino acids identical for all consensus sub-sequences. Open vertical boxes. amino acids whose homology between all consensus sub-sequences was greater than 60%. The letter "X" accounts for an amino acid whose identity level was less than 60% after the first alignment of full consensus sequences. The found dinucleotide-binding motif G266VLTGKG272 (Ref) and the dinucleotide-binding motif G313AGNVA318 (Ref) included in the N-terminal part of the Rossmann fold (β7-α8-β8) are indicated at the bottom of the frame with asterisks and circles, respectively.

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