Figure 1

Alignment of CPR aminoacid sequences. Comparison of Dictyostelium discoideum (Dd) NADPH cytochrome P450 oxidoreductase (RedA) aminoacid sequence with orthologs from Homo sapiens (Hs, P16435), Rattus norvegicus (Rn, P00388), Drosophila melanogaster (Dm, CAA63639) and Saccharomyces cerevisiae (Sc, P16603) using CLUSTAL W program. Identical and conserved amino acids are denoted with (*) and (:), respectively. Semi-conservative changes are indicated with a single dot. Binding domains for FMN, FAD and NADPH are indicated. Closed circles indicate highly conserved aromatic amino-acid residues that are particularly important in flavin binding. Open triangle points residues involved in NADPH discrimination. The ~56 aminoacid and the ~20 aminoacid hydrophobic segments at the N-terminal are indicated by dashed line in human CPR and dotted line in Dictyostelium CPR, respectively.