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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 14341: Acyl-CoA dehydrogenase family protein

There are 11 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.
 148 A0A072ZNS6 A0A072ZNS6 A0A081YFB6 A0A081YFB6 A0A0B5FI81 A0A0B5FI81 A0A0B7DEG0 A0A0B7DEG0 A0A0D0TBK6 A0A0D0TBK6
(138 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.
 66 A0A089QKU7 A0A089QKU7 A0A098FPH4 A0A098FPH4 A0A0A1DJ31 A0A0A1DJ31 A0A0A1FHT1 A0A0A1FHT1 A0A0D6FVC2 A0A0D6FVC2
(56 more...)
Isovaleryl-CoA dehydrogenase. [EC: 1.3.8.4]
Isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein.
  • Pentanoate can act as donor.
  • Formerly EC 1.3.99.10.
 60 A0A068YZ20 A0A068YZ20 A0A0A1HWN5 A0A0A1HWN5 A0A0C4Y6P7 A0A0C4Y6P7 A0A0D6T4P0 A0A0D6T4P0 A0A0E3GXW1 A0A0E3GXW1
(50 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.
 46 A0A063BN07 A0A063BN07 A0A099XKH6 A0A099XKH6 A0A0C2CFD7 A0A0C2CFD7 A0A0F7A357 A0A0F7A357 A0A0J0UY66 A0A0J0UY66
(36 more...)
Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9. [EC: 1.3.99.3]
    		40 A0A077LY24 A0A077LY24 A0A0K1ZJ67 A0A0K1ZJ67 A0A1J0II25 A0A1J0II25 A0A1J0WXG8 A0A1J0WXG8 A0A1L3DCV2 A0A1L3DCV2
    (30 more...)
    Transferred entry: 1.3.8.4. [EC: 1.3.99.10]
      		10 A0A0E9LAM9 A0A0E9LAM9 A4YSG3 A4YSG3 E8TVW5 E8TVW5 F4G7C8 F4G7C8 F4GG72 F4GG72
      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.
      		 10 A0A0H2LW51 A0A0H2LW51 A0A0P0MGV8 A0A0P0MGV8 A0A0S3PNP0 A0A0S3PNP0 A0A1E7VLK0 A0A1E7VLK0 A0A1E7X1P0 A0A1E7X1P0
      Transferred entry: 1.3.8.3. [EC: 1.3.99.21]
        		2 F6AER3 F6AER3
        Methylcrotonoyl-CoA carboxylase. [EC: 6.4.1.4]
        ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA.
          		 2 G8PXS0 G8PXS0
          Glutaryl-CoA dehydrogenase (acceptor). [EC: 1.3.99.32]
          Glutaryl-CoA + acceptor = (E)-glutaconyl-CoA + reduced acceptor.
          • The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry).
          • The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
          		 2 W7WP63 W7WP63
          Transferred entry: 1.3.8.1. [EC: 1.3.99.2]
            		2 A4YSG3 A4YSG3
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