Fig. 13.

Consensus sequences of mammalian AOX1, AOX3, AOX4 and AOX3L1 proteins. An alignment of the consensus sequences determined for mammalian AOX1, AOX3, AOX4 and AOX3L1 proteins deduced after comparison of all the available primary structures is illustrated. This alignment is based on 31 AOX1 (3 Marsupialia, 1 Hyracoydea, 1 Proboscidea, 1 Chiroptera, 2 Carnivora, 3 Artiodactyla, 1 Cetacea, 1 Perossidactyla, 2 Lagomorpha, 6 Rodentia, 10 Primates), 7 AOX3 (3 Marsupialia, 1 Proboscidea, 1 Lagomorpha, 2 Rodentia), 21 AOX4 (1 Monotreamata, 2 Marsupialia, 1 Proboscidea, 1 Chiroptera, 3 Carnivora, 1 Artiodactyla, 1 Perissodactyla, 1 Lagomorpha, 6 Rodentia, 4 Primates) and 25 AOX3L1 (2 Marsupialia, 1 Proboscidea, 1 Chiroptera, 3 Carnivora, 2 Artiodactyla, 1 Perossidactyla, 2 Lagomorpha, 6 Rodentia, 7 Primates). The AOX structural domains are indicated on the right. HR1 and HR2 = hinge regions 1 and 2. The alignment position is indicated by the numbers shown on the right. All the boxed and indicated residues are conserved across the species in at least one of the AOX isoforms. Amino acid residues specific to only one of the four AOX isoforms are circled in black. When the residues are not conserved they are indicated with an “X”. The two 2Fe/2S subdomains are indicated by a black line above the sequences. The black dots underneath the sequences of the two domains indicate the Cys residues involved in the coordination of the iron atoms. The amino acid corresponding to the non-conserved Cys residue observed in elephant AOX3L1 is indicated by a red dot. The two FAD-binding sites (FAD1 and FAD2) are indicated with a red and a dark blue line, respectively. The substrate pocket subdomains (S1–S4) are indicated above the sequences with lines of different colors. Color coding of the amino acid residues is the same as in Fig. 9