Figure 3

Amino acid alignment of GDP-D-mannose-4,6-dehydratases. The predicted amino acid sequence of schistosome GMD (Sm) is compared to GMDs of humans (Hs), Mus musculus (Mm), Danio rerio (Dr), Drosophila melanogaster (Dm), Caenorhabditis elegans (Ce-1, Ce-2), Mortierella alpina (Ma), Arabidopsis thaliana (At-1, At-2) and Bacteroides fragilis (Bf) (accession numbers in Table 1). Alignment position is indicated above each block, and sequence length is reported to the right of each line. Positions exhibiting greater than 80% conservation are highlighted in gray, and identities are identified in black. A well-conserved glycine-rich phosphate-binding loop (GxxGxxG), which is key to water-mediated hydrogen bonding between the Rossman folds of redox-associated enzymes and the pyrophosphates of dinucleotide enzyme cofactors (e.g., NAD⁺/NADP⁺) [102], is underlined. Also, the catalytically important [S/T]-Y-K triad common to members of the SDR family of enzymes is indicated by asterisks [103, 104]. Vector NTI Advance 11.0 software alignment settings: BLOSUM45 matrix, gap opening penalty = 12, gap extension penalty = 0.1, gap separation penalty range = 0, no residue-specific or hydrophobic residue gaps.