FIGURE 2.

The sequence alignment of ObcA with its homologs. The amino acid sequences of B. glumae ObcA (residues Met¹–Gly⁵⁴⁰; gene accession no. YP_002909440.1) are compared with other homologs, including those from B. gladioli (YP_004360639.1), Pseudomonas putida (ZP_19216180.1), B. pseudomallei (YP_111366.1), B. mallei (ZP_00438353.1), and B. thailandensis (ZP_02384435.1). Note that Obc1 from B. thailandensis is a bifunctional enzyme containing both ObcA and ObcB-like domains, and the identical enzymes were also identified from B. pseudomallei and B. mallei. Highly conserved residues are shown in red and boxed in blue, whereas strictly conserved residues are shown with a red background. Secondary structural elements defined in the apo form of ObcA are shown for the corresponding ObcA sequences with the N- and C-domains in blue and black, respectively. Numbers in subscript represent additional structural elements in the corresponding region of a canonical (β/α)₈-barrel fold, whereas N-domain structural elements are indicated with “N.” Residues are indicated with different notations, including the metal-coordinating residues (diamond in cyan), ligand-interacting residues (triangle in green), and acetyl-CoA interacting residues (circle in gray); in particular, the general base Tyr³²² is marked with a green star. This figure was prepared using ESPript (29).