The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Phosphatidylinositol (PI) phosphodiesterase
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 7558: Glycerophosphocholine phosphodiesterase Gde1, puta...

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Glycerophosphodiester phosphodiesterase. [EC: 3.1.4.46]
A glycerophosphodiester + H(2)O = an alcohol + sn-glycerol 3-phosphate.
  • Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolyzed.
9 A0A0F8D280 A0A0L1HG71 B9WHZ6 K0KTU4 N1NX43 Q02979 Q74ZH9 Q9C104 W1QG13
Glycerophosphocholine phosphodiesterase. [EC: 3.1.4.2]
sn-glycero-3-phosphocholine + H(2)O = choline + sn-glycerol 3-phosphate.
  • Also acts on sn-glycero-3-phosphoethanolamine.
4 G3R799 Q80VJ4 Q8C0L9 Q9NPB8
Pyruvate dehydrogenase (acetyl-transferring). [EC: 1.2.4.1]
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
  • It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
1 A0A1I7TNU7