Figure 2.

Sequence alignment of P5CRs from various sources. The following organisms are listed and square brackets indicate UniProt accession numbers: Mt, Medicago truncatula [G7KRM5], Mt_2 indicates the second isoform of MtP5CR [A2Q2Y7]; At, Arabidopsis thaliana [P54904]; Os, Oryza sativa [Q8GT01]; Ps, Pisum sativum [Q04708]; Gm, Glycine max [K7KEQ2]; So, Spinacia oleracea, only partial sequence is available (Murahama et al., 2001); Hs, Homo sapiens [P32322]; Sp, Streptococcus pyogenes [Q9A1S9]; Nm, Neisseria meningitides [Q9K1N1]. Amino acid residues are colored according to the type of residue. Numbering on the top reflects the MtP5CR sequence, while that on the right of each row is protein-specific. Residues interacting with NAD(P)⁺ and L-proline in MtP5CR structure and conserved among other species are highlighted in gray and light blue, respectively. α-Helices, 3₁₀ helices and β-strands corresponding to MtP5CR structure are depicted on top as red, blue and yellow bars, respectively. L1, L3, and L19 indicate the location of loops 1, 3, and 19, which were discussed in the paper. Seven C-terminal residues from the human P5CR sequence were omitted. The human and the two bacterial sequences were chosen for alignment as their crystal structures had already been determined.