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CATH Superfamily 1.10.540.10

Acyl-CoA dehydrogenase/oxidase, N-terminal 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:

"
Acyl-CoA dehydrogenase/oxidase, N-terminal 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 6: Acyl-coenzyme A oxidase

There are 2 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
Acyl-CoA oxidase. [EC: 1.3.3.6]
Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2).
  • Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18).
 11 A0A2J8Y161 A0A2J8Y161 P07872 P34355 Q15067 Q3SZP5 Q5RC19 Q5RC19 Q8HYL8 Q9R0H0
(1 more...)
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase. [EC: 1.17.99.3]
(25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oyl-CoA + H(2)O + acceptor = (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5- beta-cholestan-26-oyl-CoA + reduced acceptor.
  • Requires ATP.
  • The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration.
  • However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate and not via hydration of a 24(25) double bond.
  • In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate.
 4 O02767 P97562 Q99424 Q9QXD1
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