DefinePK

Abstract

The activity of 1-aminocyclopropane-1-carboxylate (ACC) deaminase enzyme and its impact on regulating ethylene concentrations and plant ACC are fundamental characteristic found in plant-associated rhizobacteria. ACC deaminase-producing bacteria, such as Pseudomonas mitigate the detrimental effects of high levels of ethylene and ACC in plant-microbe interactions, resulting in improved plant growth and development. Different species within the Pseudomonas genus are commonly found in plant microbiome worldwide. Their adaptation to the plant-associated environment makes several Pseudomonas strains highly promising for advancing novel sustainable biotechnological and agricultural solutions, particularly those exhibiting ACC deaminase activity. Thus, the present study conducted a comprehensive in silico analysis focusing on the structural and functional characteristics of ACC deaminase protein of Pseudomonas spp. The study explored correlations based on phylogenetic relatedness using both ACC deaminase enzymes and their respective genes across different Pseudomonas species and strains. This study also investigated physiochemical properties, CATH classification and STRING analysis using various bioinformatics tools. Pseudomonas brassicacearum was selected as the representative species from the Pseudomonas genus for the 3D modeling of ACC deaminase protein. The acidic ACC deaminase protein has an average molecular weight of around 25.30 kDa, with a high percentage of alpha helices in its secondary structure, demonstrating its thermal stability. This theoretical assessment of the structure and function of ACC deaminase-producing Pseudomonas could assist researchers in understanding the ACC deaminase protein, potentially facilitating a better understanding of plant-microbe interactions, and aiding in the selection of highly efficient strains for various agricultural applications.