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Figure 2 | BMC Evolutionary Biology

Figure 2

From: Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)

Figure 2

Domain and homology map of MoeB/BR/Z sequences. A. Regions of NA homology between Ps-moeZ and other sequences in this study. Homologous regions between the members of the high-homology group and Ps-moeZ are depicted as solid lines. Regions of Ps-moeZ homology to other strains are shown with dotted lines. The horizontal scale is based on the NA alignments with 0 being the first base of Mle- moeZ. B. Moving average of the ratio of the synonymous to non-synonymous nucleotide substitutions (dS/dN) per codon found among the high homology group using an 18 bp window. Scale is based on the AA alignment with 0 being the first residue of Mle- moeZ. C. Structure of MoeB/BR/Z conceptual proteins. The bars labeled with protein designations indicate the length of each structural class and the inclusion or omission of domains and motifs. ThiF = ThiF family domain; 2X CXXC = MoeB C-terminal domain containing tandem cysteine pairs, MoeBR central domain containing tandem cysteine pairs, or MoeZ central domain with modified regions in place of cysteine pairs; RHOD = Rhodanese-like domain. Locations of CXXC motifs are indicated by vertical arrows. **** = dinucleotide binding motif. (2X CXXC) = modified 2X CXXC domain. Location of E. coli MoeB residue 155 is labeled with substitutions found in each structural class within each bar. PP = Polyproline motif of MoeBR and MoeZ proteins.

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