Neff Robert J, Lages Priscilla C, Donworth Shannon K, Brien James D, Radka Christopher D
Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, KY, United States.
Front Mol Biosci. 2024 Dec 12;11:1485485. doi: 10.3389/fmolb.2024.1485485. eCollection 2024.
Oleate hydratase (OhyA), a flavoenzyme that catalyzes the hydration of unsaturated fatty acids, has been identified in various Bacillales organisms, including those in the , , , and genera. In this study, we combine structural biology with molecular and phylogenetic analyses to investigate the evolutionary dynamics of the OhyA protein family within the Bacillales order. Our evolutionary analysis reveals two distinct OhyA clades (clade I and clade II) within Bacillales that, while sharing catalytic function, exhibit significant genomic and structural differences. Our findings suggest that these OhyA clades originated from independent evolutionary processes through convergent evolution rather than gene duplication. We also show that the evolutionary divergence in OhyA is likely due to intrinsic sequence variations rather than being strictly linked to functional domain changes. Furthermore, within the genus, we observed that the evolution of the gene aligns with the species tree, supporting a common ancestral origin. This study enhances our understanding of the impact of evolutionary history on the structure and function of OhyA across the Bacillales order.
油酸水合酶（OhyA）是一种催化不饱和脂肪酸水合作用的黄素酶，已在各种芽孢杆菌目生物中被鉴定出来，包括 、 、 和 属的生物。在本研究中，我们将结构生物学与分子和系统发育分析相结合，以研究芽孢杆菌目内OhyA蛋白家族的进化动态。我们的进化分析揭示了芽孢杆菌目内两个不同的OhyA分支（分支I和分支II），它们虽然具有共同的催化功能，但在基因组和结构上存在显著差异。我们的研究结果表明，这些OhyA分支是通过趋同进化而非基因复制从独立的进化过程中产生的。我们还表明，OhyA的进化分歧可能是由于内在的序列变异，而不是严格与功能域的变化相关。此外，在 属内，我们观察到 基因的进化与物种树一致，支持共同的祖先起源。这项研究加深了我们对进化历史对芽孢杆菌目内OhyA结构和功能影响的理解。
