Alignment of a selection of FADS protein sequences used in this study (part 1 of 2). The alignment includes bifunctional FADS-type I proteins from Thermotoga maritima (Q9WZW1), Corynebacterium ammoniagenes (Q59263), Listeria monocytogenes HCC23 (YP_002350202) and Paulinella chromatophora (YP_002048796.1), FADS-type II proteins from Alistipes putredinis DSM 17216 (ZP_02425815.1), Lactobacillus plantarum JDM1 (YP_003062293.1) and Listeria monocytogenes HCC23 (YP_002350850), and plant-like FADS from Micromonas sp. RCC299 (XP_002501784), Arabidopsis thaliana L., AtRibF1 (At5g23330) and AtRibF2 (At5g08340), Carica papaya (Cp00060g00820), Populus trichocarpa (Pt07g06690, EEE90505.1), Vitis vinifera L. (Vv00g06080, XP_002273393.1), Oryza sativa L. (Os03g58710, NP_001051594), Zea mays L. (NP_001151161.1), Ricinus communis L. (XP_002517319.1), Glycine max (EST assembly from Soybean Genome Project, DoE Joint Genome Institute), Physcomitrella patens L. (Pp00229g00440, A9TH63) and Picea sitchensis L. (ABR16575.1). N-terminus (red) and C-terminus (green) within FADS proteins are marked over the sequences. Secondary structure of TmFADS (pdb 1mrz) is shown in the upper line. Predicted secondary structure of AtRibF1 is shown in the bottom line. Conserved amino acids are shown in black. Catalytic motifs in FADS enzymes are highlighted in yellow.