An Evolutionary Study in Glyphosate Oxidoreductase Gox Highlights Distinct Orthologous Groups and Novel Conserved Motifs That Can Classify Gox and Elucidate Its Biological Role.

Abstract

Glyphosate Oxidoreductase (Gox) is an enzyme known to degrade glyphosate, an intensively used wide-spectrum herbicide. Although it was first reported back in 1995, much remains unknown about its role in bacteria, its distribution across the bacterial kingdom, and its structure. This information would be valuable for better understanding the degradation pathway of glyphosate and for discovering new enzymes with the same potential. In the present study, a holistic evolutionary analysis has been performed towards identifying homologue proteins within the FAD-dependent/binding oxidoreductases family and extracting critical characteristics related to conserved protein domains and motifs that play a key role in this enzyme's function. A total of 2220 representative protein sequences from 843 species and 10 classes of bacteria were analyzed, from which 4 protein domains, 2 characteristic/functional regions, and 8 conserved motifs were identified based on multiple sequence alignment and the annotated information from biological databases. The major goal of this study is the presentation of a novel phylogenetic tree for the Gox-related proteins to identify the major protein clusters and correlate them based on their sequence, structural, and functional information towards identifying new possible pharmacological targets that are related to this specific enzyme function. Considering the lack of information about Gox, the aim of this paper is to fill in these knowledge gaps, which can help determine the biological role of Gox and consequently better understand its function.