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 14367: Long-chain specific acyl-CoA dehydrogenase

There are 5 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
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.
25 A0A069B3F1 A0A077JQ54 A0A0A1HR47 A0A0C4Y9R6 A0A0D6SBK9 A0A0E1AYM6 A0A0E1S6S5 A0A0E1UW79 A0A0E1W9Q4 A0A0F6GAL2
(15 more...)
Long-chain-acyl-CoA dehydrogenase. [EC: 1.3.8.8]
Long-chain-acyl-CoA + electron-transfer flavoprotein = long-chain-2,3- dehydroacyl-CoA + reduced electron-transfer flavoprotein.
  • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
  • The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms.
  • The highest activity was found with C(12), and the rates with C(8) and C(16) were 80% and 70%, respectively.
  • The enzyme from rat can accept substrates with C(8)-C(22).
  • It is most active with C(14) and C(16), and has no activity with C(4), C(6) or C(24).
  • cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
  • Formerly EC 1.3.99.3 and EC 1.3.99.13.
19 A0A024HMW5 A0A061IJV6 A0A077JQ54 A0A099KGY5 A0A0A8RL03 A0A0E1AYM6 A0A157V2D3 A0A1C7BMQ6 A0A1G5IC36 D7CPV9
(9 more...)
Transferred entry: 1.3.8.8. [EC: 1.3.99.13]
    12 A0A069B3F1 A0A0E1S6S5 A0A0E1UW79 A0A0E1W9Q4 A0A0F6GAL2 A3N455 A8EGG3 B1HAI3 C4KLZ2 H6RWW4
    (2 more...)
    Medium-chain acyl-CoA dehydrogenase. [EC: 1.3.8.7]
    A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-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 from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C(8) to C(12) compounds.
    • The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) compounds.
    • cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
    • Formerly EC 1.3.2.2 and EC 1.3.99.3.
    2 A0A0F7M7D0 A0A0N0E208
    Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9. [EC: 1.3.99.3]
      1 Q0VS29
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