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Enzyme Nomenclature
Information on EC 1.6.1.4 - NAD(P)+ transhydrogenase (ferredoxin)
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.6.1.4
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RECOMMENDED NAME
GeneOntology No.
NAD(P)+ transhydrogenase (ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster = NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
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SYSTEMATIC NAME
IUBMB Comments
NADH:NADP+, ferredoxin oxidoreductase
The iron-sulfur flavoprotein complex, originally isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q8U195: subunit alpha, Q8U194: subunit beta
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
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the enzyme is is necessary for effective sulfate assimilation
metabolism
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the enzyme has a key role in maintaining redox homeostasis. It is involved in maintaining the cellular redox balance, producing NADPH for biosynthesis by recycling the two other primary redox carriers, NADH and ferredoxin. The enzyme effectively couples the endergonic reduction of NADP+ by NADH and the exergonic reduction of NADP+ by reduced ferredoxin, thereby maintaining a high ratio of NADPH/NADP+ to drive biosynthesis. The Pyrococcus furiosus genome encodes an NfnI paralog termed NfnII, and the two are differentially expressed, depending on the growth conditions. Deletion of the genes encoding either NfnI or NfnII affects the cellular concentrations of NAD(P)H and particularly NADPH. This results in a moderate to severe growth phenotype in deletion mutants, demonstrating a key role for each enzyme in maintaining redox homeostasis
metabolism
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the enzyme is is necessary for effective sulfate assimilation
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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
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
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reduction of both NAD+ and Fd by Nfn enzymes is coupled to the bifurcation of electrons from NADPH oxidation. The exergonic coupling of the NADP(H) and NAD(H) half reactions in Nfn is presumed to be mediated by NADPH oxidation at L-FAD followed by electron transfer to the proximal [2Fe-2S] cluster and subsequently the NAD(H) binding site at S-FAD. Biophysical analysis of the enzyme provides the first direct insight into the mechanism of flavin-based electron bifurcation and the requisite structural features
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?
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3;
in the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+). In the absence of ferredoxin, NAD+ is only very slowly reduced (less than 1% of the rate observed in the presence of ferredoxin)
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r
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3;
in the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+). In the absence of ferredoxin, NAD+ is only very slowly reduced (less than 1% of the rate observed in the presence of ferredoxin)
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r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3;
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. In the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+)
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r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3;
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. In the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+)
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r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3;
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
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-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3;
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
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r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
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0.064 mol of NAD + is reduced per mol of enzyme per s with NADPH produced continuously by glucose-6-phosphate dehydrogenase system
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?
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
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NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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additional information
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flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
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additional information
?
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flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2 and A5N5D3
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
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-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2 and A5N5D3
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
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-
r
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
Q9X1X4
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?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
Q9X1X4
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
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the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster. The [2Fe-2S] cluster is unusual, with a relatively high (positive) reduction potential and coordination by one Asp and three Cys ligands
[4Fe-4S]-center
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the 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters
FAD
A5N5D2; A5N5D3;
iron-sulfur flavoprotein complex. Subunit NfnB contains FAD
FAD
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the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster with an unusual Asp ligand. The 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters. The L-FAD proximal [4Fe-4S] cluster coordination includes an unusual Glu ligand. S-FAD and L-FAD bind NADH and NADPH, respectively
iron-sulfur centre
A5N5D2; A5N5D3;
iron-sulfur flavoprotein complex, subunit NfnA has a predicted [2Fe2S] binding site, subunit NfnB has two predicted [4Fe4S] binding sites. UV-visible spectrum shows that the NfnAB complex contains up to 10 Fe molecules per heterodimer, which is consistent with the presence of two [4Fe4S] and one [2Fe2S] clusters
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
the enzyme contains an iron-sulfur center, a [4Fe-4S]-center, and a [2Fe-2S]-center
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KM VALUE [mM]
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.225 M NH4H2PO4, 5% (v/v) ethanol, 20% (v/v) glycerol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin column chromatography and Sephacryl S-200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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improvement of hydrogen production is achieved by overexpression of membrane-integral nicotinamide nucleotide transhydrogenase PntAB and deletion of soluble pyridine nucleotide transhydrogenase SthA. A 3.9fold increased hydrogen yield is observed
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LINKS TO OTHER DATABASES (specific for EC-Number 1.6.1.4)
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