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Information on EC 1.3.1.109 - butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)
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EC Tree
1.3.1.109 butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)IUBMB Comments
The enzyme is a complex of a flavin-containing dehydrogenase component (Bcd) and an electron-transfer flavoprotein dimer (EtfAB). The enzyme complex, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA by NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
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Word Map
- 1.3.1.109
- butyrate
- maritima
-
clostridial
-
thermotoga
- crotonyl-coa
- butanol
- dehydrogenases
-
methanogenic
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
2
=
+
2
+
2
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
=
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
Synonyms
bcd/etfab, etfab/bcd, bifurcating butyryl-coa dehydrogenase, bcd/electron-transfer flavoprotein complex, electron transferring flavoprotein/butyryl-coa dehydrogenase, butyryl-coa dehydrogenase/electron transferring flavoprotein complex, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BcdA-EtfBC
Bct/Etf complex
bifurcating butanoyl-CoA dehydrogenase
-
-
-
-
bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex
bifurcating butyryl-CoA dehydrogenase
butanoyl-CoA dehydrogenase (NAD+, ferredoxin)
-
-
-
-
butanoyl-CoA dehydrogenase/Etf complex
-
-
-
-
butyryl-CoA dehydrogenase-EtfAB complex
butyryl-CoA dehydrogenase/electron transferring flavoprotein complex
butyryl-coenzyme A dehydrogenase-EtfAB complex
electron transferring flavoprotein/butyryl-CoA dehydrogenase
Etf-Bcd complex
-
-
-
-
Etf-butyryl-CoA dehydrogenase complex
EtfAB/Bcd
bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex
Q18AQ1; Q18AQ6; Q18AQ5
-
bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex
Q18AQ1; Q18AQ6; Q18AQ5
-
-
butyryl-CoA dehydrogenase/electron transferring flavoprotein complex
-
-
butyryl-CoA dehydrogenase/electron transferring flavoprotein complex
-
-
electron transferring flavoprotein/butyryl-CoA dehydrogenase
-
electron transferring flavoprotein/butyryl-CoA dehydrogenase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, , , , , , , , , ,
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SYSTEMATIC NAME
IUBMB Comments
butanoyl-CoA:NAD+, ferredoxin oxidoreductase
The enzyme is a complex of a flavin-containing dehydrogenase component (Bcd) and an electron-transfer flavoprotein dimer (EtfAB). The enzyme complex, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA by NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
i.e. crotonyl-CoA. NADH reduces beta-FAD of electron transferring flavoprotein, which bifurcates one electron to butanoyl-CoA dehydrogenase via FAD and the other to ferredoxin. Electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 A°. The EtfAf-NAD+ complex structure reveals beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to take up one electron yielding a stable anionic semiquinone, alpha-FAD-/*, which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
i.e. crotonyl-CoA. NADH reduces beta-FAD of electron transferring flavoprotein, which bifurcates one electron to butanoyl-CoA dehydrogenase via FAD and the other to ferredoxin. Electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 A°. The EtfAf-NAD+ complex structure reveals beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to take up one electron yielding a stable anionic semiquinone, alpha-FAD-/*, which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
the enzyme couples the endergonic reduction of ferredoxin with NADH to the exergonic reduction of crotonyl-CoA to butanoyl-CoA
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
D2RIQ2; D2RIQ3; D2RL84
the electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. butanoyl-CoA dehydrogenase also contains FAD. beta-FAD of the the electron transferring flavoprotein is the acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to takeup one electron yielding a stable anionic semiquinone, alpha-FAD-/* , which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
D2RIQ2: electron transfer flavoprotein beta-subunit, D2RIQ3: electron transfer flavoprotein alpha-subunit, D2RL84: acyl-CoA dehydrogenase domain protein
D2RIQ2; D2RIQ3; D2RL84
UniProt
brenda
D2RIQ2: electron transfer flavoprotein beta-subunit, D2RIQ3: electron transfer flavoprotein alpha-subunit, D2RL84: acyl-CoA dehydrogenase domain protein
D2RIQ2; D2RIQ3; D2RL84
UniProt
brenda
Q18AQ1: Bcd2 protein, Q18AQ6: electron transfer flavoproteins subunit beta, Q18AQ5: electron transfer flavoprotein subunit alpha
Q18AQ1; Q18AQ6; Q18AQ5
UniProt
brenda
Q18AQ1: Bcd2 protein, Q18AQ6: electron transfer flavoproteins subunit beta, Q18AQ5: electron transfer flavoprotein subunit alpha
Q18AQ1; Q18AQ6; Q18AQ5
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
Q18AQ1; Q18AQ6; Q18AQ5
bifurcating butyryl-CoA dehydrogenase affects the energy yield of butyrate fermentation in the clostridial metabolism
metabolism
D2RIQ2; D2RIQ3; D2RL84
the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation
metabolism
-
the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation
-
metabolism
-
bifurcating butyryl-CoA dehydrogenase affects the energy yield of butyrate fermentation in the clostridial metabolism
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A125V4E7_CLODI
378
0
41302
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
36000
40000
-
8 * 40000 + 4 * 36000 + 4 * 28000, calculated from amino acid sequence
41000
42000
D2RIQ2; D2RIQ3; D2RL84
because electron transferring flavoprotein (EtfAf) and butanoyl-CoA dehydrogenase (BcdAf) are separated proteins in solution, a transient Bcd-Etf complex is sufficient to perform a bifurcation process. Electron transferring flavoprotein (EtfAf) is a heterodimer with a molecular mass of around 66 kDa (theoretically 37600 + 28400 Da). Butanoyl-CoA dehydrogenase (BcdAf) is homotetrameric flavoprotein (4 * 42000 Da)
28000
-
x * 41000 + x * 36000 + x * 28000, during purification the butanoyl-CoA dehydrogenase/Etf complex partially dissociated into its components, SDS-PAGE
28000
-
4 * 41000 + 2 * 36000 + 2 * 28000, calculated from amino acid sequence
28000
-
8 * 40000 + 4 * 36000 + 4 * 28000, calculated from amino acid sequence
36000
-
x * 41000 + x * 36000 + x * 28000, during purification the butanoyl-CoA dehydrogenase/Etf complex partially dissociated into its components, SDS-PAGE
36000
-
4 * 41000 + 2 * 36000 + 2 * 28000, calculated from amino acid sequence
36000
-
8 * 40000 + 4 * 36000 + 4 * 28000, calculated from amino acid sequence
41000
-
x * 41000 + x * 36000 + x * 28000, during purification the butanoyl-CoA dehydrogenase/Etf complex partially dissociated into its components, SDS-PAGE
41000
-
4 * 41000 + 2 * 36000 + 2 * 28000, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
additional information
?
-
x * 41000 + x * 36000 + x * 28000, during purification the butanoyl-CoA dehydrogenase/Etf complex partially dissociated into its components, SDS-PAGE
?
-
4 * 41000 + 2 * 36000 + 2 * 28000, calculated from amino acid sequence
?
-
8 * 40000 + 4 * 36000 + 4 * 28000, calculated from amino acid sequence
trimer
Q18AQ1; Q18AQ6; Q18AQ5
the butanoyl-CoA dehydrogenase complex is composed of the dehydrogenase and two electron-transferring flavoprotein subunits
trimer
-
the butanoyl-CoA dehydrogenase complex is composed of the dehydrogenase and two electron-transferring flavoprotein subunits
-
additional information
D2RIQ2; D2RIQ3; D2RL84
because electron transferring flavoprotein (EtfAf) and butanoyl-CoA dehydrogenase (BcdAf) are separated proteins in solution, a transient Bcd-Etf complex is sufficient to perform a bifurcation process. Electron transferring flavoprotein (EtfAf) is a heterodimer with a molecular mass of around 66 kDa (theoretically 37600 + 28400 Da). Butanoyl-CoA dehydrogenase (BcdAf) is homotetrameric flavoprotein (4 * 42000 Da)
additional information
-
because electron transferring flavoprotein (EtfAf) and butanoyl-CoA dehydrogenase (BcdAf) are separated proteins in solution, a transient Bcd-Etf complex is sufficient to perform a bifurcation process. Electron transferring flavoprotein (EtfAf) is a heterodimer with a molecular mass of around 66 kDa (theoretically 37600 + 28400 Da). Butanoyl-CoA dehydrogenase (BcdAf) is homotetrameric flavoprotein (4 * 42000 Da)
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M calcium acetate, 14 % (w/v) PEG 400, 0.1 M MES, pH 6.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D345A
the mutant shows reduced activity compared to the wild type enzyme
D345N
the mutant shows reduced activity compared to the wild type enzyme
D345A
-
the mutant shows reduced activity compared to the wild type enzyme
-
D345N
-
the mutant shows reduced activity compared to the wild type enzyme
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
although EtfAf and BcdAf are stable under air, all the experiments are performed in an anaerobic chamber under an atmosphere of 95% N2 and 5% H2, since ferredoxin and the reduced forms of flavin are oxygen-sensitive
D2RIQ2; D2RIQ3; D2RL84
732165
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 2-3 days, in the presence of FAD and under anoxic conditions the butyryl-CoA dehydrogenase/Etf complex loses 50% of its activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Strep tag II column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the electron transfer flavoprotein in Escherichia coli
D2RIQ2; D2RIQ3; D2RL84
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
engineering of Clostridum sp. MT1962 by elimination of phosphotransacetylase and acetaldehyde dehydrogenase along with integration to chromosome synthetic thiolase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase. Th resulting strain loses production of ethanol and acetate while initiated the production of 297 mM of n-butanol
synthesis
-
engineering of Clostridum sp. MT1962 by elimination of phosphotransacetylase and acetaldehyde dehydrogenase along with integration to chromosome synthetic thiolase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase. Th resulting strain loses production of ethanol and acetate while initiated the production of 297 mM of n-butanol
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, F.; Hinderberger, J.; Seedorf, H.; Zhang, J.; Buckel, W.; Thauer, R.K.
Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri
J. Bacteriol.
190
843-850
2008
Clostridium kluyveri
brenda
Aboulnaga, e.l.-.H.; Pinkenburg, O.; Schiffels, J.; El-Refai, A.; Buckel, W.; Selmer, T.
Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli
J. Bacteriol.
195
3704-3713
2013
Clostridioides difficile (Q18AQ1 and Q18AQ6 and Q18AQ5), Clostridioides difficile, Clostridioides difficile DSM 1296T (Q18AQ1 and Q18AQ6 and Q18AQ5)
brenda
Wang, S.; Huang, H.; Moll, J.; Thauer, R.K.
NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri
J. Bacteriol.
192
5115-5123
2010
Clostridium kluyveri, Clostridium kluyveri DSM 555
brenda
Chowdhury, N.P.; Mowafy, A.M.; Demmer, J.K.; Upadhyay, V.; Koelzer, S.; Jayamani, E.; Kahnt, J.; Hornung, M.; Demmer, U.; Ermler, U.; Buckel, W.
Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans
J. Biol. Chem.
289
5145-5157
2013
Acidaminococcus fermentans (D2RIQ2 and D2RIQ3 and D2RL84), Acidaminococcus fermentans DSM 20731 (D2RIQ2 and D2RIQ3 and D2RL84)
brenda
Buckel, W.; Thauer, R.K.
Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation
Biochim. Biophys. Acta
1827
94-113
2013
Clostridium kluyveri, Clostridium tetanomorphum
brenda
Mueller, N.; Schleheck, D.; Schink, B.
Involvement of NADH:acceptor oxidoreductase and butyryl coenzyme A dehydrogenase in reversed electron transport during syntrophic butyrate oxidation by Syntrophomonas wolfei
J. Bacteriol.
191
6167-6177
2009
Syntrophomonas wolfei
brenda
Berzin, V.; Tyurin, M.; Kiriukhin, M.
Selective n-Butanol production by Clostridium sp. MTButOH1365 during continuous synthesis gas fermentation due to expression of synthetic thiolase, 3-hydroxy butyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase
Appl. Biochem. Biotechnol.
169
950-959
2013
Clostridium ljungdahlii, Clostridium ljungdahlii DSM 13528
brenda
Demmer, J.K.; Pal Chowdhury, N.; Selmer, T.; Ermler, U.; Buckel, W.
The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
Nat. Commun.
8
1577
2017
Clostridioides difficile (A0A125V4E7), Clostridioides difficile, Clostridioides difficile DSM 1296 (A0A125V4E7)
brenda
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Release 2023.1 (January 2023)
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