Information on EC 1.18.1.3 - ferredoxin-NAD+ reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.18.1.3
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RECOMMENDED NAME
GeneOntology No.
ferredoxin-NAD+ reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced [2Fe-2S] ferredoxin + NAD+ + H+ = 2 oxidized [2Fe-2S] ferredoxin + NADH
show the reaction diagram
(1)
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-
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reduced 2[4Fe-4S] ferredoxin + NAD+ + H+ = oxidized 2[4Fe-4S] ferredoxin + NADH
show the reaction diagram
(2)
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-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fatty acid degradation
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oxidative phosphorylation
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NAD+ oxidoreductase
Contains FAD. Reaction (1) is written for a [2Fe-2S] ferredoxin, which is characteristic of some mono- and dioxygenase systems. The alternative reaction (2) is written for a 2[4Fe-4S] ferredoxin, which transfers two electrons, and occurs in metabolism of anaerobic bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
39369-37-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pseudomonas sp., strain KKS102
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Manually annotated by BRENDA team
strain CNRZ 510
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-
Manually annotated by BRENDA team
strain HE5
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-
Manually annotated by BRENDA team
strain HE5
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-
Manually annotated by BRENDA team
carAd or fdr gene
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Manually annotated by BRENDA team
carAd or fdr gene
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-
Manually annotated by BRENDA team
NAD-ferredocinTOL reductase component of toluene dioxygenase
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Manually annotated by BRENDA team
strain LB400
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-
Manually annotated by BRENDA team
strain NCIB 9816
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Manually annotated by BRENDA team
strain CGA009
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Manually annotated by BRENDA team
strain CGA009
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Manually annotated by BRENDA team
two different isoforms
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-
Manually annotated by BRENDA team
activity is present in wild-type strain, alcohol-adapted strain lacks detectable levels of reduced ferredoxin-linked NAD reductase
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
show the reaction diagram
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
show the reaction diagram
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
NADH + oxidized nitro blue tetrazolium + H+
NAD+ + reduced nitro blue tetrazolium
show the reaction diagram
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
show the reaction diagram
oxidized ferredoxin + NADH + H+
reduced ferredoxin + NAD+
show the reaction diagram
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
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
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
show the reaction diagram
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
show the reaction diagram
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
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enzyme enhances the level of the active form of CYP105D1
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-
?
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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in an iron-sulfur center
Iron
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iron-sulfur flavoprotein, protein contains 1.8 gatom of iron and 2.0 gatom of acid-labile sulfur
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-dipyridyl
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iodoacetate
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10 mM, 50% inhibition
KCl
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sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above
NaCl
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sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above
NEM
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10 mM, 67% inhibition
Sodium azide
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40 mM, 46% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl Co-A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046
cytochrome c
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0.0000037 - 0.0000105
Ferredoxin
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0.0105 - 0.125
NADH
0.156
NADPH
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reaction with 2,6-dichlorophenolindophenol
additional information
additional information
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Km-values for transhydrogenase reaction
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
cytochrome c
Mycobacterium sp.
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pH 8.5, 30°C
60.2
ferricyanide
Mycobacterium sp.
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pH 8.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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substrate CO-reduced ferredoxin, pH 7.7, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 7.5
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7.2
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reduction of 2,6-dichlorophenolindophenol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
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reduction of 2,6-dichlorophenolindophenol
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no activity detected at 5°C or at 55°C. Activity at 50°C is 15.2% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34900
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non-denaturing PAGE
37000
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gel filtration
39800
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x * 39800, recombinant His-tagged RedIIA, SDS-PAGE
41500
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NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, gel filtration
42396
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1 * 42396, calculated, 1 * 50000, SDS-PAGE
43000
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x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein
43600
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1 * 43600, NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, SDS-PAGE
46000
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1 * 46000, SDS-PAGE
46500
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gel filtration
50000
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gel filtration
69000
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x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant BphA4 in complex with BphA3, anaerobic crystallization is essential to crystallize the productive complex between oxidized BphA3 and NADH-reduced BphA4, sitting-drop vapour-diffusion method, 26.4 mg/ml BphA4 in 50 mM potassium phosphate buffer, pH 7.0, is reduced with 20 mM NADH for 5 min at 4°C, and mixed with oxidized BphA3 at a concentration of 17.5 mg/ml, mixing of 0.9 ml of each of the protein and reservoir solutions, and equilibration against 500 ml reservoir solution, containing 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 5.6, 30% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution
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recombinant His-tagged RedIIA from KA1, hanging-drop vapour-diffusion, 5°C, method using PEG 4000, X-ray diffraction structure determination and analysis at 1.58 A resolution, modelling
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ferredoxin reductase component of biphenyl dioxygenase
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purified recombinant enzyme, hanging-drop vapour-diffusion method, 0.001 ml of protein solution with 20mg/ml protein in 20 mM HEPES, pH 7.0, and 0.001 ml reservoir solution, containing 100 mM HEPES, pH 7.0-7.2, 16-18% w/v PEG 10 000 at 18°C, are mixed and equilibrated against 200 ml reservoir solution, 70 mM sodium cacodylate pH 6.5, 0.98 M sodium acetate, 30% v/v glycerol are best for cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using the putidaredoxin reductase structure, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
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5 d, 30% loss of activity
21
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room temperature, 8 h, 50% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 month, minimal loss of activity
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-20°C, 3 months, little loss of activity
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0-4°C, stable for up to 30 h
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0-5°C, 30% loss of activity after 5 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase
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NADH-ferredoxinNAP reductase component of naphthalene dioxygenase
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recombinant BphA4 under aerobic conditions from Escherichia coli JM109 cells by anion exchange and adsorption chromatography, and ultrafiltration
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recombinant enzyme from Escherichia col strain BL21(DE3) by repeated anion exchange chromatography, using a linear gradient of NaCl in 20 mM HEPES buffer, pH 7.0, for elution, followed by gel filtration and ultrafiltration
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recombinant His-tagged RedIIA from Escherichia coli strain BL21(DE3) by metal affinity chromatography and gel filtration
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recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both isoforms expressed in Escherichia coli BL21 StarTM (DE3) and Streptomyces lividans together with CYP105D1 from Streptomyces griseus
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expressed in Escherichia coli MV1304 as GST-fusion protein
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gene carAd or fdr, from genomic DNA, expression of His-tagged Red in Escherichia coli strain BL21(DE3)
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overexpression of BphA4 in Escherichia coli JM109 cells
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overexpression of PuR in Escherichia coli strain BL21(DE3) using the tandem tac promoters in the pCWori+ vector
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of P450-containing mono-oxygenase using purified homologous enzyme, ferrdoxin and P450
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