1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to a-ketobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition. In this work to perform comparative proteomics analysis of ACCD producing plant growth-promoting rhizobacteria (PGPR) i.e., Azospirillum lipoferum, Phyllobacterium brassicacearum, Pseudomonas fluorescens, Francisella tularensis subsp. holarctica OSU18 and Bacillus cereus. The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria.
ACCD, PGPR, α-ketobutyrate, Ammonium, Proteome, Evolutionary conservation
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