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Information on EC 1.18.1.1 - rubredoxin-NAD+ reductase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HTK9
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1.18.1.1 rubredoxin-NAD+ reductaseIUBMB 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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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(flavo)rubredoxin reductase
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-
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dihydronicotinamide adenine dinucleotide-rubredoxin reductase
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-
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DPNH-rubredoxin reductase
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-
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FIRd-reductase
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-
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NADH-rubredoxin oxidoreductase
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NADH-rubredoxin reductase
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-
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NADH: rubredoxin oxidoreductase
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NOR
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reduced nicotinamide adenine dinucleotide-rubredoxin reductase
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reductase, rubredoxin-nicotinamide adenine dinucleotide
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rubredoxin reductase
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rubredoxin-NAD reductase
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH
the electron transfer from NAD(P)H to rubredoxin involves a reductive and an oxidative step with respect to the enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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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
9032-27-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
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
-
-
?
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
rubredoxin-rubredoxin reductase complex formation, only a small number of direct interactions govern mutual recognition of RdxR and Rdx, corroborating the transient nature of the complex, overview, substrate binding structure and mechanism, the enzyme discriminates between two types of rubredoxins, RubA2 and RubA1, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
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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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the electron transfer between the enzyme and rubredoxin involves a redox active Fe3+, which can be substituted for Ni2+, mechanism, overview
additional information
-
the electron transfer between the enzyme and rubredoxin involves a redox active Fe3+, which can be substituted for Ni2+, mechanism, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, free or in complex with substrate rubredoxin, sitting drop vapour diffusion method, 20°C, 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a mutant of Pseudomonas aeruginosa with an isogenic rdxR transposon insertion is unable to grow on hexadecane
additional information
-
a mutant of Pseudomonas aeruginosa with an isogenic rdxR transposon insertion is unable to grow on hexadecane
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rdxR or PA5349, expression of His-tagged wild-type enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hagelueken, G.; Wiehlmann, L.; Adams, T.M.; Kolmar, H.; Heinz, D.W.; Tuemmler, B.; Schubert, W.D.
Crystal structure of the electron transfer complex rubredoxin-rubredoxin reductase of Pseudomonas aeruginosa
Proc. Natl. Acad. Sci. USA
104
12276-12281
2007
Pseudomonas aeruginosa (Q9HTK9), Pseudomonas aeruginosa
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