Lipase is the third most demanding enzyme group and is a major component of fat metabolism. It is omnipresent in nature. Microbial lipases are highly specific and economically efficient enzymes. They have applications in a variety of industries. In this study, the computational result elucidates structural and functional attributes of eight selected lipases from Uniprot. Primary, secondary, and tertiary structures obtained from Swiss and Profunc are analyzed. Further, they are validated with the help of Saves Server. COACH and COFACTOR is used for functional analysis. Lastly, phylogenetic tree is developed using MegaX software. Our in-silico analysis predicted lipases as alpha-beta-gamma protein with different ligand binding sites at different amino acid residue positions. Furthermore, they exhibited almost similar functional traits like catalytic activity and hydrolase activity. Overall, this study provides an insight into structural-functional characteristics of different lipases of microbial origin.