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Information on EC 1.18.1.4 - rubredoxin-NAD(P)+ reductase
for references in articles please use BRENDA:EC1.18.1.4
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EC Tree 1 Oxidoreductases
1.18 Acting on iron-sulfur proteins as donors
1.18.1 With NAD+ or NADP+ as acceptor
1.18.1.4 rubredoxin-NAD(P)+ reductase
IUBMB Comments
The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
show2
reduced rubredoxin
+
=
2
oxidized rubredoxin
+
+
Synonyms
nad(p)h-dependent rubredoxin reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD(P)-rubredoxin oxidoreductase
-
-
-
-
NAD(P)H-dependent rubredoxin reductase
NAD(P)H-rubredoxin oxidoreductase
-
-
-
-
NROR
reductase, rubredoxin-nicotinamide adenine dinucleotide (phosphate)
-
-
-
-
rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase
-
-
-
-
rubredoxin-nicotinamide adenine dinucleotide phosphate reductase
-
-
-
-
NROR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced rubredoxin + NAD(P)+ = 2 oxidized rubredoxin + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
rubredoxin:NAD(P)+ oxidoreductase
The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized.
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CAS REGISTRY NUMBER
COMMENTARY
114514-31-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
Substrates: cytochrome c from horse heart
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?
2 oxidized rubredoxin + NADH
2 reduced rubredoxin + NAD+ + H+
-
Substrates: -
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?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+ + H+
-
Substrates: -
Products: -
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?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH
?
-
Substrates: -
Products: -
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?
benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
Substrates: -
Products: -
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?
Fe(III) citrate + NADH
Fe(II) citrate + NAD+
-
Substrates: -
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?
methyl viologen + NADH
reduced methyl viologen + NAD+ + H+
-
Substrates: -
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?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
Substrates: -
Products: -
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?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+ + H+
Substrates: -
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?
oxidized benzyl viologen + NADPH
reduced benzyl viologen + NADP+
-
Substrates: -
Products: -
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?
oxidized benzyl viologen + NADPH
reduced benzyl viologen + NADP+ + H+
Substrates: -
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?
oxidized Clostridium pasteurianum rubredoxin + NADH
reduced Clostridium pasteurianum rubredoxin + NAD+ + H+
oxidized Clostridium pasteurianum rubredoxin + NADPH
reduced Clostridium pasteurianum rubredoxin + NADP+ + H+
oxidized Pyrococcus furiosus rubredoxin + NADH
reduced Pyrococcus furiosus rubredoxin + NAD+ + H+
-
Substrates: -
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?
oxidized Pyrococcus furiosus rubredoxin + NADPH
reduced Pyrococcus furiosus rubredoxin + NADP+ + H+
-
Substrates: -
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?
oxidized rubredoxin + NADH
reduced rubredoxin + NAD+
-
Substrates: rubredoxin is the best substrate
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?
oxidized rubredoxin + NADPH
reduced rubredoxin + NADP+
-
Substrates: -
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?
oxidized rubredoxin + NADPH
reduced rubredoxin + NADP+ + H+
-
Substrates: -
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r
oxidized rubrerythrin + NADH
reduced rubrerythrin + NAD+ + H+
-
Substrates: -
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?
oxidized rubrerythrin + NADPH
reduced rubrerythrin + NADP+ + H+
-
Substrates: -
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
-
Substrates: -
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
Substrates: -
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
-
Substrates: rubredoxin is the most efficient electron acceptor
Products: -
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
Substrates: superoxide reductase mediates reduction of superoxide to hydrogen peroxide in an NADPH-dependent manner via a coupled reaction between NAD(P)H:rubredoxin oxidoreductase, rubredoxin, and superoxide reductase
Products: -
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?
oxidized Clostridium pasteurianum rubredoxin + NADH
reduced Clostridium pasteurianum rubredoxin + NAD+ + H+
-
Substrates: -
Products: -
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?
oxidized Clostridium pasteurianum rubredoxin + NADH
reduced Clostridium pasteurianum rubredoxin + NAD+ + H+
-
Substrates: -
Products: -
Products: -
?
oxidized Clostridium pasteurianum rubredoxin + NADPH
reduced Clostridium pasteurianum rubredoxin + NADP+ + H+
-
Substrates: -
Products: -
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?
oxidized Clostridium pasteurianum rubredoxin + NADPH
reduced Clostridium pasteurianum rubredoxin + NADP+ + H+
-
Substrates: -
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?
oxidized flavodiiron protein + NADH
reduced flavodiiron protein + NAD+ + H+
-
Substrates: -
Products: -
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?
oxidized flavodiiron protein + NADH
reduced flavodiiron protein + NAD+ + H+
-
Substrates: -
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?
oxidized flavodiiron protein + NADPH
reduced flavodiiron protein + NADP+ + H+
-
Substrates: -
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?
oxidized flavodiiron protein + NADPH
reduced flavodiiron protein + NADP+ + H+
-
Substrates: -
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?
additional information
?
-
-
Substrates: the enzyme has no activity with ferredoxins, flavodoxins, and thioredoxins
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?
additional information
?
-
-
Substrates: the enzyme has no activity with ferredoxins, flavodoxins, and thioredoxins
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?
additional information
?
-
-
Substrates: the enzyme does not reduce Pyrococcus furiosus ferredoxin
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 oxidized rubredoxin + NADH
2 reduced rubredoxin + NAD+ + H+
-
Substrates: -
Products: -
Products: -
?
oxidized rubredoxin + NADPH
reduced rubredoxin + NADP+
-
Substrates: -
Products: -
Products: -
?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
-
Substrates: rubredoxin is the most efficient electron acceptor
Products: -
Products: -
?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
Substrates: superoxide reductase mediates reduction of superoxide to hydrogen peroxide in an NADPH-dependent manner via a coupled reaction between NAD(P)H:rubredoxin oxidoreductase, rubredoxin, and superoxide reductase
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
the catalytic efficiency exhibited by this enzyme for NADH is higher than for NADPH
NADPH
-
the catalytic efficiency exhibited by this enzyme for NADH is higher than for NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no substrate inhibition at high NAD(P)H (up to 0.3 mM)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the enzyme contains one flavin adenine dinucleotide (FAD) molecule per mol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0028
oxidized Clostridium pasteurianum rubredoxin
-
with NADPH as cosubstrate, at pH 7.0 and 30Ā°C
-
0.0043
oxidized Clostridium pasteurianum rubredoxin
-
with NADH as cosubstrate, at pH 7.0 and 30Ā°C
-
0.0032
oxidized Pyrococcus furiosus rubredoxin
-
with NADPH as cosubstrate, at pH 7.0 and 30Ā°C
-
0.0052
oxidized Pyrococcus furiosus rubredoxin
-
with NADH as cosubstrate, at pH 7.0 and 30Ā°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3 - 6
oxidized Clostridium pasteurianum rubredoxin
-
with NADH as cosubstrate, at pH 7.0 and 30Ā°C
-
13.9
oxidized Clostridium pasteurianum rubredoxin
-
with NADPH as cosubstrate, at pH 7.0 and 30Ā°C
-
9.6
oxidized Pyrococcus furiosus rubredoxin
-
with NADPH as cosubstrate, at pH 7.0 and 30Ā°C
-
69.4
oxidized Pyrococcus furiosus rubredoxin
-
with NADH as cosubstrate, at pH 7.0 and 30Ā°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5000
oxidized Clostridium pasteurianum rubredoxin
-
with NADPH as cosubstrate, at pH 7.0 and 30Ā°C
-
8400
oxidized Clostridium pasteurianum rubredoxin
-
with NADH as cosubstrate, at pH 7.0 and 30Ā°C
-
3000
oxidized Pyrococcus furiosus rubredoxin
-
with NADPH as cosubstrate, at pH 7.0 and 30Ā°C
-
13000
oxidized Pyrococcus furiosus rubredoxin
-
with NADH as cosubstrate, at pH 7.0 and 30Ā°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 80
-
about 70fold increase in kcat/Km for oxidized rebredoxin increases from 25Ā°C to 80Ā°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme is possibly a part of a defense mechanism against oxygen toxicity
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NROR_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
359
0
39941
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
when the organism is grown on maltose plus S(0) the specific activity of the enzyme is highest under this growth condition, slightly lower on the maltose-only medium, and lower still in the three peptide-based media
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, K.; Adams, M.W.W.
NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus
Methods Enzymol.
334
55-62
2001
Pyrococcus furiosus
brenda
Grunden, A.M.; Jenney, F.E.; Ma, K.; Ji, M.; Weinberg, M.V.; Adams, M.W.
In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus
Appl. Environ. Microbiol.
71
1522-1530
2005
Pyrococcus furiosus (Q8U1K9)
brenda
Ma, K.; Adams, M.W.
A hyperactive NAD(P)H:rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
181
5530-5533
1999
Pyrococcus furiosus
brenda
Cabeza, M.; Guerrero, S.; Iglesias, A.; Arias, D.
New enzymatic pathways for the reduction of reactive oxygen species in Entamoeba histolytica
Biochim. Biophys. Acta
1850
1233-1244
2015
Entamoeba histolytica, Entamoeba histolytica HM1-IMSS
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus
brenda
EXTERNAL LINKS (specific for EC-Number 1.18.1.4)
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Release 2023.1 (January 2023)
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