Information on EC 1.3.1.109 - butanoyl-CoA dehydrogenase (NAD+, ferredoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.109
-
RECOMMENDED NAME
GeneOntology No.
butanoyl-CoA dehydrogenase (NAD+, ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
butanoyl-CoA:NAD+, ferredoxin oxidoreductase
This flavin containg enzyme, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA with NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
D2RIQ2: electron transfer flavoprotein beta-subunit, D2RIQ3: electron transfer flavoprotein alpha-subunit, D2RL84: acyl-CoA dehydrogenase domain protein
D2RIQ2 and D2RIQ3 and D2RL84
UniProt
Manually annotated by BRENDA team
D2RIQ2: electron transfer flavoprotein beta-subunit, D2RIQ3: electron transfer flavoprotein alpha-subunit, D2RL84: acyl-CoA dehydrogenase domain protein
D2RIQ2 and D2RIQ3 and D2RL84
UniProt
Manually annotated by BRENDA team
Peptoclostridium difficile
Q18AQ1: Bcd2 protein, Q18AQ6: electron transfer flavoproteins subunit beta, Q18AQ5: electron transfer flavoprotein subunit alpha
Q18AQ1 and Q18AQ6 and Q18AQ5
UniProt
Manually annotated by BRENDA team
Q18AQ1: Bcd2 protein, Q18AQ6: electron transfer flavoproteins subunit beta, Q18AQ5: electron transfer flavoprotein subunit alpha
Q18AQ1 and Q18AQ6 and Q18AQ5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
show the reaction diagram
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
show the reaction diagram
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
Butanoyl-CoA
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
pH 7.5, 22-25C
0.012
NADH
D2RIQ2 and D2RIQ3 and D2RL84
pH 7, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 8
Butanoyl-CoA
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
pH 7.5, 22-25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2800
Butanoyl-CoA
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
pH 7.5, 22-25C
802
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
D2RIQ2 and D2RIQ3 and D2RL84
assay at
7.5
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23 - 25
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
320000
-
gel filtration
574000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
D2RIQ2 and D2RIQ3 and D2RL84
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
FMN can not substitute for FAD in stabilizing the enzyme activity
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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 and D2RIQ3 and D2RL84
732165
oxygen-stable
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
725287
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Peptoclostridium difficile
Q18AQ1 and Q18AQ6 and Q18AQ5
expression of the electron transfer flavoprotein in Escherichia coli
D2RIQ2 and D2RIQ3 and D2RL84