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Information on EC 1.6.1.4 - NAD(P)+ transhydrogenase (ferredoxin)
for references in articles please use BRENDA:EC1.6.1.4
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EC Tree 1 Oxidoreductases
1.6 Acting on NADH or NADPH
1.6.1 With NAD+ or NADP+ as acceptor
1.6.1.4 NAD(P)+ transhydrogenase (ferredoxin)
IUBMB Comments
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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
show+
+
2
+
2
=
+
2
+
2
+
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
=
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
Synonyms
nadh-dependent reduced ferredoxin:nadp+ oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ferredoxin: NAD(P)H oxidoreductase
ferredoxin:NADP+ oxidoreductase
FprA
NADH-dependent reduced ferredoxin:NADP oxidoreductase
NADH-dependent reduced ferredoxin:NADP+ oxidoreductase
NfnAB
NADH-dependent reduced ferredoxin:NADP+ oxidoreductase
A5N5D2; A5N5D3
-
-
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: 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
Products: -
Products: -
?
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
additional information
?
-
-
Substrates: flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
Products: -
Products: -
?
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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)
Products: -
Products: -
r
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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)
Products: -
Products: -
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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+)
Products: -
Products: -
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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+)
Products: -
Products: -
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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
Products: -
Products: -
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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
Products: -
Products: -
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: 0.064 mol of NAD + is reduced per mol of enzyme per s with NADPH produced continuously by glucose-6-phosphate dehydrogenase system
Products: 0.064 mol of NAD + is reduced per mol of enzyme per s with NADPH produced continuously by glucose-6-phosphate dehydrogenase system
?
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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; A5N5D3
Substrates: 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
Products: -
Products: -
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
A5N5D2; A5N5D3
Substrates: 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
Products: -
Products: -
r
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
Substrates: -
Products: -
Products: -
?
NADH + H+ + NADP+ + reduced ferredoxin [iron-sulfur] cluster
NAD+ + NADPH + oxidized ferredoxin [iron-sulfur] cluster
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
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
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
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q8U195: subunit alpha, Q8U194: subunit beta
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the enzyme is is necessary for effective sulfate assimilation
metabolism
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
-
the enzyme is is necessary for effective sulfate assimilation
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PYRKH_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
282
0
31091
Swiss-Prot
-
SUDHA_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
474
0
52729
Swiss-Prot
-
SUDHB_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
278
0
30817
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurokawa, T.; Fukumori, Y.; Yamanaka, T.
Purification of a flavoprotein having NADPH-cytochrome c reductase and transhydrogenase activities from Nitrobacter winogradskyi and its molecular and enzymatic properties
Arch. Microbiol.
148
95-99
1987
Nitrobacter winogradskyi, Nitrobacter winogradskyi ATCC 14123
-
brenda
Wang, S.; Huang, H.; Moll, J.; Thauer, R.K.
NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri
J. Bacteriol.
192
5115-5123
2010
Clostridium kluyveri (A5N5D2 and A5N5D3), Clostridium kluyveri DSM 555 (A5N5D2 and A5N5D3)
brenda
Cho, H.; Kim, Y.; Min, B.; Jung, G.; Park, J.
Improvement of hydrogen production yield by rebalancing NADPH/NADH ratio in a recombinant Escherichia coli
J. Nanoelectr. Optoelectr.
6
343-347
2011
Escherichia coli
-
brenda
Tian, L.; Lo, J.; Shao, X.; Zheng, T.; Olson, D.; Lynd, L.
Ferredoxin NAD+ oxidoreductase of Thermoanaerobacterium saccharolyticum and its role in ethanol formation
Appl. Environ. Microbiol.
82
7134-7141
2016
Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum LL1025
brenda
Lewis, T.; Glassing, A.; Harper, J.; Franklin, M.
Role for ferredoxin NAD(P)H oxidoreductase (FprA) in sulfate assimilation and siderophore biosynthesis in pseudomonads
J. Bacteriol.
195
3876-3887
2013
Pseudomonas putida, Pseudomonas putida DSM 3601
brenda
Demmer, J.K.; Huang, H.; Wang, S.; Demmer, U.; Thauer, R.K.; Ermler, U.
Insights into flavin-based electron bifurcation via the NADH-dependent reduced ferredoxin NADP oxidoreductase structure
J. Biol. Chem.
290
21985-21995
2015
Thermotoga maritima (Q9X1X4), Thermotoga maritima ATCC 43589 (Q9X1X4)
brenda
Nguyen, D.M.N.; Schut, G.J.; Zadvornyy, O.A.; Tokmina-Lukaszewska, M.; Poudel, S.; Lipscomb, G.L.; Adams, L.A.; Dinsmore, J.T.; Nixon, W.J.; Boyd, E.S.; Bothner, B.; Peters, J.W.; Adams, M.W.W.
Two functionally distinct NADP+-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosus
J. Biol. Chem.
292
14603-14616
2017
Pyrococcus furiosus (Q8U195 and Q8U194)
brenda
Lubner, C.E.; Jennings, D.P.; Mulder, D.W.; Schut, G.J.; Zadvornyy, O.A.; Hoben, J.P.; Tokmina-Lukaszewska, M.; Berry, L.; Nguyen, D.M.; Lipscomb, G.L.; Bothner, B.; Jones, A.K.; Miller, A.F.; King, P.W.; Adams, M.W.W.; Peters, J.W.
Mechanistic insights into energy conservation by flavin-based electron bifurcation
Nat. Chem. Biol.
13
655-659
2017
Pyrococcus furiosus (Q8U195 and Q8U194)
brenda
EXTERNAL LINKS (specific for EC-Number 1.6.1.4)
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