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geosmin synthase has alpha-alpha domain architecture. The N-terminal domain and the C-terminal domain are separated by a 41-residue linker and share 28% and 29% amino acid sequence identity, respectively, with pentalenene synthase. Each domain contains characteristic metal ion-binding motifs of class I terpenoid cyclases. The aspartate-rich motif is found as D86DHFLE91 and D455DYYP459, and the NSE/DTE motif is found as N229DLFSYQRE237 and N598DVFSYQKE606. The C-terminal domain is also predicted to adopt an alpha fold homologous to that of the N-terminal domain based on approximately 36% amino acid sequence identity between these domains. Primary, secondary and quarternary enzyme structrue analysis, and homology modeling, overview
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