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CATH Superfamily 1.20.140.10

Butyryl-CoA Dehydrogenase, subunit A, domain 3

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 3
".

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 4: Acyl-CoA dehydrogenase FadE25

There are 3 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.
 9 E5KSD5 E5KSD5 P15651 P16219 P16219 P79273 Q07417 Q3ZBF6 Q5RAS0
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
Acryloyl-CoA reductase (NADH). [EC: 1.3.1.95]
Propanoyl-CoA + NAD(+) = acryloyl-CoA + NADH.
  • The reaction is catalyzed in the opposite direction to that shown.
  • The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF).
  • The ETF is reduced by NADH and transfers the electrons to the active site.
  • Catalyzes a step in a pathway for L-alanine fermentation to propanoate.
  • Cf. EC 1.3.1.84.
 1 G3KIM8