The goal of the study was to partially establish the role of a putative terpene synthase gene (snas_1127) identified from a soil-dwelling Gram-positive, filamentous actinobacteria, Stackebrandtia nassauensis DSM 44728 by genome mining to be a functional germacradienol synthase enzyme. The snas_1127 gene of S. nassauensis was cloned by PCR and heterologously expressed in Escherichia coli as an N-terminal-His6-tag protein. Incubation of the recombinant protein, SNAS_1127, with farnesyl diphosphate (FPP) in the presence of Mg2+ gave a sesquiterpene germacradienol; a precursor for many industrially important terpene metabolites. However, the bioinformatics analysis revealed that the target protein contains two conserved domains, viz. C-terminal domain and N-terminal domain. It is already established that the C-terminal domain catalyzed the conversion of farnesyl pyrophosphate (FPP) to germacradienol and thus germacradienol serves as a substrate for the N-terminal domain and gets converted to geosmin. On manual comparison of the identified protein sequence with already characterized germacradienol/ geosmin synthases, it was observed that there is a point mutation in the NSE triad (274E instead of the usual 274D) of the N-terminal domain. This might be why SNGS catalyzed only the conversion of FPP to germacradien-4-ol, and due to point mutation, the further conversion didn’t go as expected. Therefore, no other identifiable products were observed on GC-MS. As SNGS catalyzed the conversion of FPP to germacradienol, which being the precursor for the synthesis of many industrially useful metabolites, can be synthesized in a controlled manner without the risk of further conversion by the N-terminal domain. PhD Research in a Bird-eye View