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Significance Our studies demonstrate that Vip1 represents a rare class of bifunctional enzyme capable of synthesizing and destroying signaling molecules important for nutrient adaptation, cellular architecture, and organelle morphology. We find that Vip1 contains two tethered autonomous catalytic active sites, which modulate levels of 1-IP7 and 1,5-IP8 through 1-kinase and 1-pyrophosphatase domains. Each activity is critical for maintaining the highly dynamic anabolic and catabolic regulation of cellular pools of IP7 and IP8 . That this occurs through a single gene product emphasizes that Vip1 is a key metabolic switch critical for cellular adaptation.

Vip1 is a kinase and pyrophosphatase switch that regulates inositol diphosphate signaling