Abstract
5-enolpyruvylshikimate 3-phosphate synthase (EPSPS) is the central enzyme of the shikimate pathway to synthesize three aromatic amino acids in fungi, plants and prokaryotes. This enzyme is the target of the herbicide glyphosate. In most plants and prokaryotes, the EPSPS protein is constituted by a single domain, whereas in fungi, it contains several EPSPS-associated domains. Here, we perform a comprehensive analysis of 390 EPSPS proteins of fungi to determine the distribution and the evolution of the EPSPS-associated domains. The results of this study will be useful to determine the potential differential impact of glyphosate on alternative domain architectures in fungi.
Highlights
The enolpyruvylshikimate-3-phosphate synthase (EPSPS)-associated domains can be classified into four partially overlapping groups (Figure 1): shikimate, enzymes, expression and structural function
The analysis of the EPSPS-associated domains across fungal species shows that they are mostly involved in the shikimate pathway (e.g., SKI, DHQ_synthase, DHquinase_I) and in the synthesis of aromatic amino acids (e.g., Shikimate_dh_N, PDH)
An evolutionary analysis shows that the ancestral state of the EPSPS protein included six domains (DHQ synthase, EPSPS, SKI, DHquinase I, shikimate DH N and shikimate DH)
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Glyphosate, the most used herbicide against weeds, and glyphosate-based products (GBPs), target the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) [1,2]. EPSPS ( known as aroA) is the central enzyme in the shikimate pathway for the synthesis of three essential amino acids [3]. The enzyme is present in plants and prokaryotes as a single-domain protein, and in fungi as a multi-domain protein [4,5]. As the enzyme is not found in animals, the use of glyphosate is supposed to be safe for human health
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