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Soluble inorganic pyrophosphatases (PPases) are constitutive enzymes catalyzing the hydrolysis of inorganic pyrophosphate (PPi). This housekeeping reaction provides the driving force for numerous biosynthetic processes, including protein and DNA synthesis; this makes PPases absolutely indispensable enzymes for any living organism and, hence, attractive targets for the development of cytotoxic agents. Family I PPases include both eukaryotic and prokaryotic representatives. Their active site high conservation presents the major obstacle preventing targeting Family I PPases from pathogenic species for antimicrobial therapy. Some functional peculiarities of PPase from Mycobacterium tuberculosis (Mt-PPase) may be a basis for the development of its selective inhibitors. In this work, we made a systematic research on the characterization of the observed variability within Family I PPases using structural bioinformatics and computational approaches.