FIG. 1.

Sequence analyses of T. vaginalis α-enolase. T. vaginalis tv-ENO1 was compared to the enolase enzymes of parasites, fungi, bacteria, and humans. The amino acid sequence identity values of T. vaginalis tv-ENO1 to the enolase enzymes of Trypanosoma brucei, Leishmania major, Saccharomyces cerevisiae, Candida albicans, Streptococcus pneumoniae, E. coli, and Homo sapiens as listed vertically were 74%, 69%, 84%, 65%, 76%, 65%, and 67%, respectively. Active sites are marked with an asterisk (amino acids E₂₅₅, K₃₈₉, and H₄₁₇), and the positions of metal-binding residues are labeled zero (amino acids S₇₈, D₂₉₂, E₃₃₇, and D₃₆₄). The enolase finger print motif is boxed within amino acids 75 to 84, and the domain for hydrophobic putative signal peptides is indicated by a bar and a bracket (amino acids 416 to 423). Gaps introduced to maximize alignment are indicated by dashes.