Information on EC 1.18.1.8 - ferredoxin-NAD+ oxidoreductase (Na+-transporting)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.18.1.8
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RECOMMENDED NAME
GeneOntology No.
ferredoxin-NAD+ oxidoreductase (Na+-transporting)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NAD+ oxidoreductase (Na+-transporting)
This iron-sulfur and flavin-containing electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD+ by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cluster rnf1 and rnf2
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Manually annotated by BRENDA team
gene cluster rnfCDGEAB
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Manually annotated by BRENDA team
rnfABCDEF gene cluster
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Manually annotated by BRENDA team
gene cluster rnf
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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iron limitation in Rhodobacter capsulatus leads to an increase in cellular levels of RnfB
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + NAD+ + H+ + Na+in
2 oxidized ferredoxin + NADH + Na+out
show the reaction diagram
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
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-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
show the reaction diagram
2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
show the reaction diagram
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-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
show the reaction diagram
additional information
?
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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
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
show the reaction diagram
2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
show the reaction diagram
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-
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-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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flavin
iron-sulfur centre
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iron–sulfur and flavin-containing electron transport complex
methanophenazine
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[4Fe-4S]-center
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
subunit RnfB contains 4Fe-4S clusters
additional information
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subunits RnfD and RnfG both contain the same motif, suggesting that they bind flavins in a similar way, mass spectroscopic analysis, overview. The flavins in RnfG and RnfD are localized in the periplasmic space
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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KCl itself has no effect on Na+ transport, in combination with valinomycin Na+ transport is stimulated slightly
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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complete inhibition of Na+ transport at 0.5 mM
Ag+
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complete inhibition of Na+ transport at 0.1 mM
Cu2+
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complete inhibition of Na+ transport at 0.08 mM
diphenyleniodonium chloride
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complete inhibition of Na+ transport at 0.04 mM
diphenyliodonium chloride
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complete inhibition of Na+ transport at 0.04 mM
additional information
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the enzyme complex is inhibited by sodium ionophores but not protonophores, demonstrating a direct coupling of the ferredoxin:NAD+ oxidoreductase activity to Na+ transport
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ETH2120
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reduced ferredoxin:NAD+ oxidoreductase activity at inverted membrane vesicles is not stimulated to 155% of control
monensin
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reduced ferredoxin:NAD+ oxidoreductase activity at inverted membrane vesicles is not stimulated to 138% of control
valinomycin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.155 - 2.5
Na+/in
0.085
NAD+
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pH 7.7, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.155
1,10-phenanthroline
Acetobacterium woodii
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.00375
Ag+
Acetobacterium woodii
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.00175
Cu2+
Acetobacterium woodii
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.000035
diphenyleniodonium chloride
Acetobacterium woodii
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.001
diphenyliodonium chloride
Acetobacterium woodii
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
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Manually annotated by BRENDA team
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RnfH might be a soluble protein
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Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21400
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
21600
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
22800
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
26000
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1 * 26000, recombinant isolated subunit RnfG, SDS-PAGE, 1 * 39000, recombinant isolated subunit RnfD, SDS-PAGE
35000
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
36600
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
39000
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1 * 26000, recombinant isolated subunit RnfG, SDS-PAGE, 1 * 39000, recombinant isolated subunit RnfD, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
hexamer
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
recombinant wild-type and mutant His-tagged RnfD and RnfG fom Vibrio cholerae cells by nickel affinity chromatography and gel filtration
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Rnf complex with 6 components
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cluter rnfCDGEAB
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gene rnfC, encoded in the rnfABCDEF cluster
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genes rnfD and rnfG, cloning of Rnf complex subunits and recombinant individual expression of wild-type and mutant His-tagged RnfD and RnfG in Vibrio cholerae cells producing protein fluorescence under UV illumination, recombinant subunit protein topology analysis, overview
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RnfC and RnfG are overproduced in Escherichia coli
C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T175L
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site-directed mutagenesis of subunit RnfG, the mutation affects FMN cofactor binding
T187V
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site-directed mutagenesis of subunit RnfD, the mutation affects flavin cofactor binding
T278L
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site-directed mutagenesis of subunit RnfD, the mutation does not affect flavin cofactor binding
T175L
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site-directed mutagenesis of subunit RnfG, the mutation affects FMN cofactor binding
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T187V
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site-directed mutagenesis of subunit RnfD, the mutation affects flavin cofactor binding
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T278L
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site-directed mutagenesis of subunit RnfD, the mutation does not affect flavin cofactor binding
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