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CATH Superfamily 1.10.8.870

Alpha-glycerophosphate oxidase, cap domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Alpha-glycerophosphate oxidase, cap domain
".

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 22: Glycerol-3-phosphate dehydrogenase

There are 1 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
Glycerol-3-phosphate dehydrogenase. [EC: 1.1.5.3]
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
  • An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis.
  • In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane.
  • In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain.
  • This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix.
  • Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9).
  • The enzyme is activated by calcium.
  • Formerly EC 1.1.2.1 and EC 1.1.99.5.
 4 L8ATW3 L8ATW3 P74257 P74257
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