Acinetobacter baumannii is a species of gram-negative, rod-shaped bacteria belonging to the Acinetobacter genus. It is a well-known notorious pathogen and is commonly found in various environments such as in soil, water, and hospital wastewater. This study focused on characterizing A. baumannii through 16S RNA sequencing and computationally investigating the potential of peroxidase enzyme for its ability to degrade pyrethroid compounds, which are commonly found in insecticides. In this study, homology modeling predicted the 3D structure of protein and Expasy ProtParam was used to analyze the physical characteristics of the protein. Additionally, the ERRAT value of 96.24 and Ramachandran plot analysis revealed that 93.7% of the residues were present in the most favored region further confirming the stability of the protein. Moreover, molecular docking analysis was performed to evaluate the binding free energy between the peroxidase protein and pyrethroid compounds. Notably, etofenprox exhibited the highest binding energy at − 9.6 kcal/mol followed by biphenthrin, beta-cyfluthrin, D-phenothrin, and tetramethrin which exhibited same binding energy of − 9.3 kcal/mol, indicating potential interactions with the protein as well. Overall, this study provides insights into the potential enzymatic degradation of pyrethroid compounds by the peroxidase protein from A. baumannii. These findings contribute to the understanding of the molecular interactions involved in the degradation process and may provide ideas for the development of eco-friendly and efficient strategies as well as for managing pyrethroid-contaminated environments.