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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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 28 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
Crotonobetainyl-CoA reductase. [EC: 1.3.8.13]
Gamma-butyrobetainyl-CoA + electron-transfer flavoprotein = crotonobetainyl-CoA + reduced electron-transfer flavoprotein.
  • The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21.
  • The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes.
 268 A0A026V735 A0A028AH90 A0A028DNC6 A0A029IFK5 A0A029J3K7 A0A070FAU3 A0A070SRX4 A0A070UXT3 A0A073G3J6 A0A073HVR2
(258 more...)
Nitrite reductase (cytochrome; ammonia-forming). [EC: 1.7.2.2]
NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+).
  • The enzyme also reduces nitric oxide and hydroxylamine to ammonia, and sulfite to sulfide.
 263 A0A015VFK0 A0A015YEK3 A0A015YEM7 A0A016F5Z1 A0A017PBD5 A0A028AMB2 A0A028DIW7 A0A029HCM0 A0A029IG29 A0A061LMQ9
(253 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.
 91 A0A069XL85 A0A070SKQ7 A0A070UJQ5 A0A0D6HEU1 A0A0E1LVB8 A0A0E1NVA1 A0A0E1SY65 A0A0F6AXB6 A0A0F6BZ88 A0A0F7J3Q6
(81 more...)
Acyl-CoA oxidase. [EC: 1.3.3.6]
Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2).
  • Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18).
 90 A0A0W0DSJ9 A0A0W0DSJ9 A0A178UA38 A0A178UA38 A0A178WDE4 A0A178WDE4 A0A1H6PLL8 A0A1H6PLL8 A0A1H6PV70 A0A1H6PV70
(80 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.
 84 A0A069XL85 A0A070SKQ7 A0A070UJQ5 A0A0D6HEU1 A0A0E1LVB8 A0A0E1NVA1 A0A0E1SY65 A0A0F6AXB6 A0A0F6BZ88 A0A0F7J3Q6
(74 more...)
4-hydroxyphenylacetate 3-monooxygenase. [EC: 1.14.14.9]
4-hydroxyphenylacetate + FADH(2) + O(2) = 3,4-dihydroxyphenylacetate + FAD + H(2)O.
  • The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds.
  • The enzyme uses FADH(2) as a substrate rather than a cofactor.
  • FADH(2) is provided by EC 1.5.1.36.
  • Formerly EC 1.14.13.3.
 16 A0A069QC19 A0A164XWI6 A0A1G5GZ05 A0A2V2TZ52 A0A2X1V1M2 A4IT51 C0SPC0 G4EVK5 L8AIQ5 Q48440
(6 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.
 15 A0A1M6MZ63 A0A2P8MHH2 E5KSD5 G0VLZ7 P15651 P16219 P52042 P79273 Q06319 Q07417
(5 more...)
L-prolyl-[peptidyl-carrier protein] dehydrogenase. [EC: 1.3.8.14]
L-prolyl-[peptidyl-carrier protein] + 2 electron-transfer flavoprotein = 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] + 2 reduced electron- transfer flavoprotein.
  • The enzyme participates in the biosynthesis of several pyrrole- containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1.
  • It is believed to catalyze the formation of a Delta(2)-pyrrolin-2- yl(carbonyl)-S-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].
 12 A0A1H2D2L0 A0A2C9EM00 A0A2I5TBS1 A0A2P8AHC1 A0A397QC92 A0A3E0GMD7 A0A423ECW1 D6ENZ3 O54143 Q4KCY6
(2 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.
 11 A0A0A0MT83 P12007 P26440 P34275 Q0WPE4 Q3SZI8 Q5RBD5 Q75IM9 Q9FS87 Q9JHI5
(1 more...)
Very-long-chain acyl-CoA dehydrogenase. [EC: 1.3.8.9]
A very-long-chain acyl-CoA + electron-transfer flavoprotein = a very- long-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 is most active toward long-chain acyl-CoAs such as C(14), C(16) and C(18), but is also active with very-long-chain acyl-CoAs up to 24 carbons.
  • It shows no activity for substrates of less than 12 carbons.
  • It's specific activity toward palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase.
  • cf. EC 1.3.8.1, EC 1.3.8.7 and EC 1.3.8.8.
  • Formerly EC 1.3.99.3.
 10 P45953 P45953 P48818 P48818 P49748 P49748 P50544 P50544 Q8HXY7 Q8HXY7
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase. [EC: 1.17.99.3]
(25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oyl-CoA + H(2)O + acceptor = (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5- beta-cholestan-26-oyl-CoA + reduced acceptor.
  • Requires ATP.
  • The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration.
  • However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate and not via hydration of a 24(25) double bond.
  • In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate.
 8 O02767 O02767 P97562 P97562 Q99424 Q99424 Q9QXD1 Q9QXD1
Glutaryl-CoA dehydrogenase (ETF). [EC: 1.3.8.6]
Glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO(2) + reduced electron-transfer flavoprotein.
  • The enzyme catalyzes the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5).
  • FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle.
  • The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyzes the oxidation to glutaconyl-CoA (EC 1.3.99.32).
  • Formerly EC 1.3.99.7.
 8 A0A024R7F9 P81140 Q20772 Q2KHZ9 Q54R47 Q60759 Q8HXX8 Q92947
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.
 7 A0A0S2Z3P9 P45954 P70584 Q54RR5 Q5EAD4 Q5RF40 Q9DBL1
3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase. [EC: 1.14.14.12]
3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMNH(2) + O(2) = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMN + H(2)O.
  • This bacterial enzyme participates in the degradation of several steroids, including cholesterol and testosterone.
  • It can use either FADH or FMNH(2) as flavin cofactor.
  • The enzyme forms a two-component system with a reductase (HsaB) that utilizes NADH to reduce the flavin, which is then transferred to the oxygenase subunit.
 6 A0A045I4W3 A0A0H3LG75 A5U8P5 P9WJA0 P9WJA1 Q0S811
4-nitrophenol 2-monooxygenase. [EC: 1.14.13.29]
4-nitrophenol + NADH + O(2) = 4-nitrocatechol + NAD(+) + H(2)O.
    		 4 D0FZR3 I0WZP1 Q6F4M8 Q8RQQ0
    4-nitrocatechol 4-monooxygenase. [EC: 1.14.13.166]
    4-nitrocatechol + NAD(P)H + O(2) = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)(+) + H(2)O.
    • The enzyme catalyzes the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite.
    • Forms a two-component system with a flavoprotein reductase.
    • The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyze EC 1.14.13.29, while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyze EC 1.14.13.167.
    		 3 D0FZR3 I0WZP1 Q6F4M8
    (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.
    		 3 A0A1H5TAJ7 A0A2R4BRK4 Q9KJE8
    Nitroalkane oxidase. [EC: 1.7.3.1]
    A nitroalkane + H(2)O + O(2) = an aldehyde or ketone + nitrite + H(2)O(2).
    • While nitroethane may be the physiological substrate, the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols.
    • Differs from EC 1.13.12.16 in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates.
    		 2 B2AM55 Q8X1D8
    4-hydroxybutanoyl-CoA dehydratase. [EC: 4.2.1.120]
    4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H(2)O.
    • The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation, Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation, and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO(2) fixation pathway found in some thermoacidophilic archaea.
    		 1 P55792
    (2S)-methylsuccinyl-CoA dehydrogenase. [EC: 1.3.8.12]
    (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein = 2-methylfumaryl-CoA + reduced electron-transfer flavoprotein.
    • The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation.
    		 1 D3JV03
    Cyclohexane-1-carbonyl-CoA dehydrogenase (electron-transfer flavoprotein). [EC: 1.3.8.11]
    Cyclohexane-1-carbonyl-CoA + electron-transfer flavoprotein = cyclohex-1- ene-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 Q2LQP0
    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
    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.
    		 1 C3UVB0
    Vinylacetyl-CoA Delta-isomerase. [EC: 5.3.3.3]
    Vinylacetyl-CoA = (E)-but-2-enoyl-CoA.
    • Also acts on 3-methyl-vinylacetyl-CoA.
    		 1 P55792
    Anthranilate 3-monooxygenase (FAD). [EC: 1.14.14.8]
    Anthranilate + FADH(2) + O(2) = 3-hydroxyanthranilate + FAD + H(2)O.
    • This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation.
    • The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which ensures ample supply of FAD to the monooxygenase.
    		 1 A4IT51
    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
    2-methylacyl-CoA dehydrogenase. [EC: 1.3.99.12]
    2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor.
    • Also oxidizes 2-methylpropanoyl-CoA.
    • Not identical with EC 1.3.8.1, EC 1.3.8.7, EC 1.3.8.8 or EC 1.3.8.9.
    		 1 Q9FS88
    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