InterPro domain: IPR017946

This superfamily represents a structural domain consisting of a TIM beta/alpha-barrel. These domains are found in several phospholipase C (PLC) like phosphodiesterases, including:

• Mammalian phospholipase C isozyme D1 [ 1 ].
• Bacterial phosphatidylinositol-specific phospholipase C [ 2 ].
• Glycerophosphodiester phosphodiesterases, such as GlpQ from Escherichia coli and UgpQ from Agrobacterium tumefaciens [ 3 ].

Phospholipase C (PLC) isozymes are directly activated by heterotrimeric G proteins and Ras-like GTPases to hydrolyse phosphatidylinositol 4,5-bisphosphate into the second messengers diacylglycerol and inositol 1,4,5-trisphosphate. PLC enzymes often play central roles in various signalling cascades [ 4 ].

1. C2 domain conformational changes in phospholipase C-delta 1. Nat. Struct. Biol. 3, 788-95
2. Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis. Biochemistry 36, 12802-13
3. Crystal structure of glycerophosphodiester phosphodiesterase from Agrobacterium tumefaciens by SAD with a large asymmetric unit. Proteins 65, 514-8
4. General and versatile autoinhibition of PLC isozymes. Mol. Cell 31, 383-94