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Enzyme Nomenclature
Information on EC 1.6.1.4 - NAD(P)+ transhydrogenase (ferredoxin)
Word Map on EC 1.6.1.4
- 1.6.1.4
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bifurcation
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flavin-based
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thermoanaerobacterium
- saccharolyticum
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endergonic
- synthesis
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The enzyme appears in viruses and cellular organisms
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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, 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
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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
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
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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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?
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
A5N5D2 and 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 and 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 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. 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 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. 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 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
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+ + 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
-
-
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
A5N5D2 and 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
FAD
A5N5D2 and A5N5D3
iron-sulfur flavoprotein complex. Subunit NfnB contains FAD
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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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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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