Functional Annotation of Hypothetical Protein From <i>Delftia acidovorans</i> Having Role in PFAS Biodegradation and Bioremediation Potential

ABSTRACT Perfluorinated and polyfluorinated alkyl substances (PFAS) are manmade compounds that persist in the environment, defy decomposition, and accumulate in living beings. Global focus on PFAS degradation pathways is due to its hazards of environmental pollution, immune system disruption, liver damage, hormone abnormalities, and others. A gram‐negative bacillus from PFAS‐contaminated soils, Delftia acidovorans , may grow slightly with PFOA as a carbon source, suggesting a dehalogenase enzyme can break down the chemicals. This study will describe and annotate a hypothetical protein D. acidovorans ' function (Accession no. WP_011137954.1). A comprehensive insilico approach was used for physicochemical characterization, functional annotation, subcellular localization, energy minimization, and protein structure prediction. According to domain, family, and superfamily links, evolutionary correlations, and sequence similarity, the protein dehalogenates. After active site prediction, molecular docking showed that PFAS compounds PFDA (Perfluorodecanoic acid), PFNA (Perfluorononanoic acid), and PFOS (Perfluorooctanesulfonic acid) gave −7.9, −7.7, and −7.3 kcal/mol binding affinity. Molecular dynamics simulations validated the stability and flexibility of the ligand and protein, with RMSD values ranging from 1.4 to 2.5 Å and RMSF values indicating minor structural changes in the protein. This research suggests that a putative protein working as a dehalogenase in D. acidovorans might be a biotechnological target for bioremediation to improve environmental safety and sustainability.