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[Display omitted] • Novel isoprene degrading Arthrobacter sp. strain BHU FT2 was sequenced. • Potential degradation pathway enzymes were identified. • Molecular docking gave high affinity of pathway enzymes for respective substrates. • Novel high sequence identity monooxygenase with known isoprene monooxygenase obtained. • In-vitro analysis on hydrocarbons displayed high specificity of isolate for isoprene. The bacterial degradation of isoprene is important for maintaining its atmospheric concentration in unpolluted environment. It may be possible to use natural isoprene degrading bacteria in engineered systems to eliminate or limit isoprene emissions from various sources. Biodegradation of isoprene by Arthrobacter sp. strain BHU FT2 was investigated. The genome was found to contain 4151545 bp long chromosome having 3747 coding genes, and coded potential isoprene degrading enzymes. The molecular docking of monooxygenases with isoprene displayed a higher binding energy (−4.59 kcal/mol) for WP_015938387.1 monooxygenase. Analysis of the identified monooxygenases with the known isoprene monooxygenases revealed 67% sequence identity of WP_015938387.1 (Locus tag JHV56_10705) monooxygenase of the considered strain with the OPX16961.1 monooxygenase of Gordonia sp. i37 isoprene degrading starin. These results provided a strong evidence for the high isoprene degrading potential of the Arthrobacter sp. BHU FT2 which could be efficiently exploited for isoprene degradation in large scale bio-filtration units. [ABSTRACT FROM AUTHOR]