In Silico Molecular Insights on the Structure-Function Aspects of ACC Deaminase of a Non-Pathogenic Klebsiella Pneumoniae

Abstract

Bacterial 1-aminocyclopropane-1-carboxylic acid deaminase (ACCD) is known to involve in breaking down the 1-aminocyclopropane-1-carboxylic acid (ACC), immediate precursor of ethylene, into a-ketobutyrate and ammonia. This is required when stress (biotic or abiotic) induced ethylene content is accelerated in plant cells resulting in reduction in plant biomass and yield. Klebsiellapneumoniae, although previously considered only as a pathogenic bacteria, there are some strains reported till date to prove it as a plant growth promoting bacteria (PGPB). ACCD activity has reported from the said strain but the present study is emphasized on its molecular proteomic structures and functions studied in silico. The present work revealed that the ACCD of K. pneumoniae is a 36.5 kDatetrameric stable protein found in intracellular condition. The phylogenetic analysis clearly depicts its similarity with several other ACCD reported from different bacterial genera. The structure-function insight would definitely help future researchers in designing wet lab as well as dry lab experiments.