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CATH Superfamily 2.40.110.10

Butyryl-CoA Dehydrogenase, subunit A, domain 2

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:

"
Butyryl-CoA Dehydrogenase, subunit A, domain 2
".

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 3336: Putative acyl-CoA dehydrogenase FadE1

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
(R)-benzylsuccinyl-CoA dehydrogenase. [EC: 1.3.8.3]
(R)-2-benzylsuccinyl-CoA + electron-transfer flavoprotein = (E)-2- benzylidenesuccinyl-CoA + reduced electron-transfer flavoprotein.
  • Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate- and enantiomer specificity it is highly specific for (R)- benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA.
  • Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica.
  • Ferricenium ion is an effective artificial electron acceptor.
  • Formerly EC 1.3.99.21.
 23 A0A045I1H0 A0A083WME3 A0A0G4E2Q5 A0A0H3M2L2 A0A0H3P754 A0A0K2HRX2 A0A0T7LCD2 A0A0T7PCA9 A0A0T9CDH5 A0A0T9EAW9
(13 more...)
Short-chain acyl-CoA dehydrogenase. [EC: 1.3.8.1]
A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
  • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
  • The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms.
  • The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms.
  • The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA.
  • The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA.
  • Cf. EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9.
  • Formerly EC 1.3.2.1 and EC 1.3.99.2.
 2 A0A0H3L4M3 A0A1L7MCR9
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