Information on EC 1.18.1.1 - rubredoxin-NAD+ reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.18.1.1
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RECOMMENDED NAME
GeneOntology No.
rubredoxin-NAD+ reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH
show the reaction diagram
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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octane oxidation
SYSTEMATIC NAME
IUBMB Comments
rubredoxin:NAD+ oxidoreductase
Requires FAD. The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin. The reaction does not occur when NADPH is substituted for NADH. Contains iron at the redox centre.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-27-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains TBCF10839 and PAO1, gene PA5349 or rdxR
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
NROR is a versatile electron donor for scavengers of O2 and reactive oxygen species
additional information
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the enzyme's disulfide bonds are not involved in the electron transfer from NADH to rubredoxin catalyzed by NROR
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
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weak activity
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
show the reaction diagram
NADH + 2-methyl-1,4-naphthoquinone
NAD+ + 2-methyl-1,4-naphthoquinol
show the reaction diagram
-
-
-
-
?
NADH + Fe(CN)63-
NAD+ + Fe(CN)64-
show the reaction diagram
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-
-
-
?
NADH + H+ + 1,4-naphthoquinone
NAD+ + 1,4-naphthoquinol
show the reaction diagram
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-
-
-
?
NADH + H+ + oxidized rubredoxin-2
NAD+ + reduced rubredoxin
show the reaction diagram
NADH + H+ + oxiized methyl thiazolyl tetrazolium
NAD+ + reduced methyl thiazolyl tetrazolium
show the reaction diagram
NADH + metmyoglobin
NAD+ + reduced metmyoglobin
show the reaction diagram
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-
-
-
?
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
show the reaction diagram
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weak activity
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
show the reaction diagram
NADH + p-benzoquinone
NAD+ + p-benzoquinol
show the reaction diagram
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-
-
-
?
NADH + p-iodonitrotetrazolium
NAD+ + reduced p-iodonitrotetrazolium
show the reaction diagram
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-
-
-
?
NADH + p-toluoquinone
NAD+ + p-toluoquinol
show the reaction diagram
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-
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-
?
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
show the reaction diagram
reduced rubredoxin + NAD+
oxidized rubredoxin + NADH
show the reaction diagram
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-
-
-
?
additional information
?
-
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 + oxidized rubredoxin
NAD+ + reduced rubredoxin
show the reaction diagram
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
show the reaction diagram
Q9HTK9
the enzyme and two rubredoxins form a system indipensable for metabolizing n-alkanes, they constitute an electron transport pathway that shuttles reducing equivalents from carbon metabolism to the membrane-bound alkane hydroxylases AlkB1 and AlkB2
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?
reduced rubredoxin + NAD+
oxidized rubredoxin + NADH
show the reaction diagram
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-
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
binding site structure, overview
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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redox and spectroscopic properties of non-heme diiron site
additional information
the electron transfer between the enzyme and rubredoxin involves a redox active Fe3+, which can be substituted for Ni2+, mechanism, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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2,4-dinitrophenol
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8-hydroxyquinoline
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AgNO3
NaCl
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70 mM, 50% inhibition
p-hydroxymercuribenzoate
p-mercuribenzoate
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Sodium arsenite
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Sodium mersalyl
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Tetrodotoxin
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thionicotinamide-NAD+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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addition of FAD increases activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
2,6-dichloroindophenol
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0.055
Fe(CN)63-
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0.11 - 1.6
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.42
Desulfovibrio gigas rubredoxin
Desulfovibrio gigas
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
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rubredoxin-dependent reduction of cytochrome c
82
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rubredoxin-dependent reduction of cytochrome c
86
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rubredoxin-dependent reduction of cytochrome c
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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phosphate buffer
8.5
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Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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x * 27000 + x * 32000, SDS-PAGE
32000
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x * 27000 + x * 32000, SDS-PAGE
38000
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gel filtration
50500
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1 * 50500, SDS-PAGE
55300
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calculation from sedimenation and diffusion measurement
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
RdxR consists of two cofactor-binding domains and a C-terminal domain essential for the specific recognition of Rdx, crystal structure analysis, dimerization restricts access to the NAD(P)H binding pocket and results in a steric clash between the modeled adenine moiety of NAD(P)H and alpha-helix alpha8' of the neighboring molecule, RdxR dimers form at high protein concentrations used during crystallization, rather than being functionally relevant, overview
monomer
additional information
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enzyme interacts with its physiological partner NADH:flavorubredoxin oxidoreductase. Redox properties and mechanism of electron transfer are fine-tuned upon the interaction
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme, sitting-drop vapour-diffusion method, 20C, 0.001 l of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.0, is mixed with 0.001 ml of reservoir solution containing 35% v/v PEG 400, 0.1 M Tris-HCl, pH 8.5, and 0.15 M MgCl2, and equilibrated against 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.1 A resolution
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purified recombinant His6-tagged enzyme, sitting-drop vapour-diffusion method, 20C, 0.001 l of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.0, is mixed with 0.001 ml of reservoir solution containing 35% v/v PEG 400, 0.1 M Tris-HCl, pH 8.5, and 0.15 M MgCl2, and equilibrated against 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.1 A resolution, structure modelling, overview
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purified recombinant His-tagged enzyme, free or in complex with substrate rubredoxin, sitting drop vapour diffusion method, 20C, 8.5 mg/ml protein in 100 mM NaCl, 50 mM Tris-HCl, pH 8.0, FAD, and 5 mM 2-mercaptoethanol, in presence or absence of rubredoxin in a 1.2 molar excess, mixing with an equal volume of reservoir solution containing 5% PEG 1000, 40% PEG 300, 0.1 M Tris-HCl, pH 7.0, mother liquor supplemented with 25% PEG 400 is used for cryoprotection, X-ray diffraction structure determination and analysis at 2.3-2.4 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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5 min, no inactivation in presence of FAD
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% glycerol protects against inactivation, prevents loss of FAD from the intact enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli to homogeneity
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recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amplification from genomic DNA, overexpression as His6-tagged protein in Escherichia coli strain Tuner (DE3)
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expressed in Escherichia coli TG1
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expression in Escherichia coli
gene rdxR or PA5349, expression of His-tagged wild-type enzyme in Escherichia coli
overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
NROR is an O2-inducible protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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