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Information on EC 1.18.1.1 - rubredoxin-NAD+ reductase and Organism(s) Clostridium acetobutylicum and UniProt Accession Q9AL95

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IUBMB Comments
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.
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Clostridium acetobutylicum
UNIPROT: Q9AL95
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Word Map
The taxonomic range for the selected organisms is: Clostridium acetobutylicum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
reduced rubredoxin
+
+
=
oxidized rubredoxin
+
Synonyms
rubredoxin reductase, nadh:rubredoxin oxidoreductase, nadh rubredoxin oxidoreductase, nadh-rubredoxin oxidoreductase, (flavo)rubredoxin reductase, nad(p)h:rubredoxin reductase, reduced nicotinamide adenine dinucleotide-rubredoxin reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADH:rubredoxin oxidoreductase
-
(flavo)rubredoxin reductase
-
-
-
-
dihydronicotinamide adenine dinucleotide-rubredoxin reductase
-
-
-
-
DPNH-rubredoxin reductase
-
-
-
-
FIRd-reductase
-
-
-
-
NADH-rubredoxin oxidoreductase
-
-
-
-
NADH-rubredoxin reductase
-
-
-
-
NADH: rubredoxin oxidoreductase
-
-
-
-
NOR
-
-
-
-
reduced nicotinamide adenine dinucleotide-rubredoxin reductase
-
-
-
-
reductase, rubredoxin-nicotinamide adenine dinucleotide
-
-
-
-
rubredoxin reductase
-
-
-
-
rubredoxin-NAD reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
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
-
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 + H+ + 1,4-naphthoquinone
NAD+ + 1,4-naphthoquinol
show the reaction diagram
-
-
-
-
?
NADH + metmyoglobin
NAD+ + reduced metmyoglobin
show the reaction diagram
-
-
-
-
?
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
show the reaction diagram
-
weak activity
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
show the reaction diagram
NADH + p-benzoquinone
NAD+ + p-benzoquinol
show the reaction diagram
-
-
-
-
?
NADH + p-iodonitrotetrazolium
NAD+ + reduced p-iodonitrotetrazolium
show the reaction diagram
-
-
-
-
?
NADH + p-toluoquinone
NAD+ + p-toluoquinol
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
the induction of rubredoxin reductase, normally observed at pH 4.3 is stopped immediately after the addition of rifampicin. The enzyme could play a role in some deacidification mechanism in relation to proton transport
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
binding structure, overview
NADH
binding structure, overview
FAD
-
prosthetic group
NADPH
-
no significant reaction with
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2,4-dinitrophenol
-
-
p-hydroxymercuribenzoate
-
-
sodium arsenite
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
-
rubredoxin-dependent reduction of cytochrome c
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
gel filtration
41000
-
1 * 41000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
NROR exists as a monomer in solution, the overall structure of NROR displays a GR-fold
monomer
-
1 * 41000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme, sitting-drop vapour-diffusion method, 20°C, 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
purified recombinant His6-tagged enzyme, sitting-drop vapour-diffusion method, 20°C, 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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplification from genomic DNA, overexpression as His6-tagged protein in Escherichia coli strain Tuner (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
NROR is an O2-inducible protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petitdemange, H.; Marczak, R.; Blusson, H.; Gay, R.
Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum
Biochem. Biophys. Res. Commun.
91
1258-1265
1979
Clostridium acetobutylicum
Manually annotated by BRENDA team
Marczak, R.; Ballongue, J.; Petitdemange, H.; Gay, R.
Regulation of the biosynthesis of NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum
Curr. Microbiol.
10
165-168
1984
Clostridium acetobutylicum
-
Manually annotated by BRENDA team
Nishikawa, K.; Shomura, Y.; Kawasaki, S.; Niimura, Y.; Higuchi, Y.
Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum
Acta Crystallogr. Sect. F
66
23-25
2010
Clostridium acetobutylicum (Q9AL95), Clostridium acetobutylicum
Manually annotated by BRENDA team
Nishikawa, K.; Shomura, Y.; Kawasaki, S.; Niimura, Y.; Higuchi, Y.
Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum: A key component of the dioxygen scavenging system in obligatory anaerobes
Proteins
78
1066-1070
2010
Clostridium acetobutylicum (Q9AL95), Clostridium acetobutylicum
Manually annotated by BRENDA team