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Myo Inositol 1-Phosphate Synthase (MIPS), which catalyzes the first step of inositol metabolism, has been reported from a diverse range of organism like bacteria to human including different groups of plants and animals. The present work is carried out to explore and analyze structural forms of the respective MIPS proteins from complete sequenced genome or proteome available on database of one representative from two important plant groups viz. bryophyte ( Physcomitrella patens ) and pteridophyte ( Selaginella moellendorffii ). Previously reported characteristic MIPS sequences was used to identify it’s homolog ones from those members under study. The explored sequences compared with a number of MIPS varieties from other plant members to study the conserveness or evolution of the protein/enzyme. ProtParam tool provided necessary theoretical physicochemical data of the predicted proteins, the three-dimensional structures were predicted through homology modelling with identified amino acid data. Structural evaluation and stereochemical analyses were performed using ProSA-web displaying Z-scores and Molprobity visualising Ramachandran plot.

Computational Fishing and Structural Analysis of MIPS Protein from Two Important Plant Groups