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

EC NUMBER
COMMENTARY hide
1.6.1.4
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RECOMMENDED NAME
GeneOntology No.
NAD(P)+ transhydrogenase (ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster = NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A5N5D2: NfnA, A5N5D3: NfnB
A5N5D2, A5N5D3
UniProt
Manually annotated by BRENDA team
A5N5D2: NfnA, A5N5D3: NfnB
A5N5D2, A5N5D3
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Q8U195: subunit alpha, Q8U194: subunit beta
SwissProt
Manually annotated by BRENDA team
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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
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
show the reaction diagram
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
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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
show the reaction diagram
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
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
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
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flavoprotein
iron-sulfur centre
[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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
NAD+
A5N5D2; A5N5D3;
pH 7, 37°C
0.025
NADPH
A5N5D2; A5N5D3;
pH 7, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
A5N5D2; A5N5D3;
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
A5N5D2; A5N5D3;
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.225 M NH4H2PO4, 5% (v/v) ethanol, 20% (v/v) glycerol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin column chromatography and Sephacryl S-200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
expression in Escherichia coli
A5N5D2; A5N5D3;
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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