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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_3_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 1: Acyl-CoA dehydrogenase, mitochondrial

There are 4 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
2-methyl-branched-chain-enoyl-CoA reductase. [EC: 1.3.8.5]
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut- 2-enoyl-CoA + reduced electron-transfer flavoprotein + H(+).
  • From Ascaris suum.
  • The reaction functions in shuttling reducing power from the electron- transport chain to 2-methyl branched-chain enoyl CoA.
  • Formerly EC 1.3.1.52.
 9 A0A0S2Z3P9 A0A0S2Z3P9 P45954 P45954 P70584 Q54RR5 Q5EAD4 Q5RF40 Q9DBL1
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.
 9 E5KSD5 E5KSD5 P15651 P16219 P16219 P79273 Q07417 Q3ZBF6 Q5RAS0
Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase. [EC: 1.3.8.10]
Cyclohex-1-ene-1-carbonyl-CoA + electron-transfer flavoprotein = (E)-2- cyclohex-1,5-diene-1-carbonyl-CoA + reduced electron-transfer flavoprotein.
  • The enzyme, characterized from the strict anaerobic bacterium Syntrophus aciditrophicus, is involved in production of cyclohexane- 1-carboxylate, a byproduct produced by that organism during fermentation of benzoate and crotonate to acetate.
 1 Q2LQN9
Caffeoyl-CoA reductase. [EC: 1.3.1.108]
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD(+) + 2 reduced ferredoxin [iron-sulfur] cluster = (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster.
  • The enzyme, characterized from the bacterium Acetobacterium woodii, couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant.
  • It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
  • It also reduces 4-coumaroyl-CoA and feruloyl-CoA.
 1 H6LGM6