BRENDA - Enzyme Database show
show all sequences of 1.6.1.4

NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri

Wang, S.; Huang, H.; Moll, J.; Thauer, R.K.; J. Bacteriol. 192, 5115-5123 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Clostridium kluyveri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.025
-
NADPH
pH 7, 37°C
Clostridium kluyveri
1
-
NAD+
pH 7, 37°C
Clostridium kluyveri
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Clostridium kluyveri
5737
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
Clostridium kluyveri
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
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
Clostridium kluyveri DSM 555
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
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium kluyveri
A5N5D2 and A5N5D3
A5N5D2: NfnA, A5N5D3: NfnB
-
Clostridium kluyveri DSM 555
A5N5D2 and A5N5D3
A5N5D2: NfnA, A5N5D3: NfnB
-
Purification (Commentary)
Commentary
Organism
-
Clostridium kluyveri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
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)
731998
Clostridium kluyveri
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
-
-
-
r
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
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)
731998
Clostridium kluyveri DSM 555
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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
731998
Clostridium kluyveri
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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
731998
Clostridium kluyveri DSM 555
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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+)
731998
Clostridium kluyveri
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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+)
731998
Clostridium kluyveri DSM 555
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
-
-
-
r
Subunits
Subunits
Commentary
Organism
heterodimer
-
Clostridium kluyveri
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Clostridium kluyveri
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Clostridium kluyveri
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
iron-sulfur flavoprotein complex. Subunit NfnB contains FAD
Clostridium kluyveri
iron-sulfur centre
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
Clostridium kluyveri
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Clostridium kluyveri
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
iron-sulfur flavoprotein complex. Subunit NfnB contains FAD
Clostridium kluyveri
iron-sulfur centre
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
Clostridium kluyveri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.025
-
NADPH
pH 7, 37°C
Clostridium kluyveri
1
-
NAD+
pH 7, 37°C
Clostridium kluyveri
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Clostridium kluyveri
5737
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
Clostridium kluyveri
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
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
Clostridium kluyveri DSM 555
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
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Clostridium kluyveri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
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)
731998
Clostridium kluyveri
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
-
-
-
r
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
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)
731998
Clostridium kluyveri DSM 555
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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
731998
Clostridium kluyveri
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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
731998
Clostridium kluyveri DSM 555
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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+)
731998
Clostridium kluyveri
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
-
-
-
r
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster
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+)
731998
Clostridium kluyveri DSM 555
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
-
Clostridium kluyveri
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Clostridium kluyveri
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Clostridium kluyveri
Other publictions for EC 1.6.1.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745371
Nguyen
Two functionally distinct NAD ...
Pyrococcus furiosus
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292
14603-14616
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1
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1
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1
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1
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745843
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Pyrococcus furiosus
Nat. Chem. Biol.
13
655-659
2017
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1
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-
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-
1
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-
1
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-
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-
1
1
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3
-
-
-
-
-
1
3
-
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-
-
-
-
-
-
-
-
-
-
-
-
1
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-
1
1
-
-
-
-
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-
-
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741703
Tian
Ferredoxin NAD+ oxidoreductas ...
Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum LL1025
Appl. Environ. Microbiol.
82
7134-7141
2016
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-
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-
-
-
1
-
2
-
2
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-
-
-
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2
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1
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2
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2
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742880
Demmer
Insights into flavin-based el ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
J. Biol. Chem.
290
21985-21995
2015
-
-
1
1
-
-
-
-
-
1
-
2
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
2
1
-
-
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-
-
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-
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-
742779
Lewis
Role for ferredoxin NAD(P)H o ...
Pseudomonas putida, Pseudomonas putida DSM 3601
J. Bacteriol.
195
3876-3887
2013
-
-
-
-
-
-
-
-
-
1
-
2
-
2
-
-
-
-
-
-
-
-
2
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-
-
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-
1
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1
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1
-
2
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-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
734518
Cho
-
Improvement of hydrogen produc ...
Escherichia coli
J. Nanoelectr. Optoelectr.
6
343-347
2011
-
1
1
-
-
-
-
-
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1
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-
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1
1
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-
-
-
-
731998
Wang
NADP+ reduction with reduced f ...
Clostridium kluyveri, Clostridium kluyveri DSM 555
J. Bacteriol.
192
5115-5123
2010
-
-
1
-
-
-
-
2
1
-
-
2
-
2
-
-
1
-
-
-
-
-
6
1
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
2
1
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
288551
Kurokawa
-
Purification of a flavoprotein ...
Nitrobacter winogradskyi, Nitrobacter winogradskyi ATCC 14123
Arch. Microbiol.
148
95-99
1987
-
-
-
-
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2
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3
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1
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1
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3
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