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Information on EC 1.19.1.1 - flavodoxin-NADP+ reductase
for references in articles please use BRENDA:EC1.19.1.1
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EC Tree 1 Oxidoreductases
1.19 Acting on reduced flavodoxin as donor
1.19.1 With NAD+ or NADP+ as acceptor
1.19.1.1 flavodoxin-NADP+ reductase
IUBMB Comments
A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin—NADP+ reductase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
bacterial ferredoxin-NADP+ reductase, BaFPR, Bc_0385, EcFPR, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin/flavodoxin NADP+ oxidoreductase 1, ferredoxin/flavodoxin NADP+ oxidoreductase 2, ferredoxin/flavodoxin NADP+ oxidoreductase 3, ferredoxin/flavodoxin-NADP(H) oxidoreductase, Flavodoxin reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bacterial ferredoxin-NADP+ reductase
Bc_0385
ferredoxin/flavodoxin-NADP(H) oxidoreductase
flavodoxin/ferredoxin-NADP reductase
FLDR
FNR
FPR
PETH
YumC
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
-
-
-
-
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
the bacterial ferredoxin-NADP+ reductase shows a catalytic mechanism with a particular NADP+ binding mode
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
the bacterial ferredoxin-NADP+ reductase shows a catalytic mechanism with a particular NADP+ binding mode
A0A7T5QNX4
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
the bacterial ferredoxin-NADP+ reductase shows a catalytic mechanism with a particular NADP+ binding mode
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
the bacterial ferredoxin-NADP+ reductase shows a catalytic mechanism with a particular NADP+ binding mode
-
-
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
the bacterial ferredoxin-NADP+ reductase shows a catalytic mechanism with a particular NADP+ binding mode
-
-
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SYSTEMATIC NAME
IUBMB Comments
flavodoxin:NADP+ oxidoreductase
A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin---NADP+ reductase.
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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
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
Substrates: -
Products: -
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?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
Substrates: -
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?
reduced flavodoxin 1 + NADP+
oxidized flavodoxin 1 + NADPH + H+
-
Substrates: -
Products: -
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?
reduced flavodoxin 2 + NADP+
oxidized flavodoxin 2 + NADPH + H+
-
Substrates: -
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?
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
Substrates: -
Products: -
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?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
Substrates: -
Products: -
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?
reduced flavodoxin-like protein NrdI + NADP+
oxidized flavodoxin-like protein NrdI + NADPH + H+
-
Substrates: -
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?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
Substrates: -
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?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
Substrates: -
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?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
Substrates: -
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?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
Substrates: -
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?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
-
Substrates: -
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?
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+ + H+
Substrates: -
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?
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+ + H+
-
Substrates: -
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?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
Substrates: -
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?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
Substrates: -
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?
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
-
Substrates: -
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r
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
-
Substrates: -
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r
oxidized cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
Substrates: -
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r
oxidized cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
Substrates: -
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
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?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
A0A7T5QNX4
Substrates: -
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r
additional information
?
-
-
Substrates: interaction analysis of two flavodoxins (Fld1-2), one flavodoxin-like protein (NrdI), and three different thioredoxin reductase (TrxR)-like FNRs (FNR1-3), steady-state kinetics, overview. A large-scale conformational rearrangement takes place during the FNR catalytic cycle to allow for the binding and reduction of the Fld and, subsequently, the re-reduction of the FNR by NADPH. The flavodoxins are structurally similar. No reduction of the Fld under aerobic conditions
Products: -
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?
additional information
?
-
Substrates: Brucella abortus FNR (EcFPR) contains 0.30 NADP+/FNR (mol/mol)
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?
additional information
?
-
Substrates: Brucella abortus FNR (EcFPR) contains 0.30 NADP+/FNR (mol/mol)
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?
additional information
?
-
Substrates: the enzyme reduces flavodoxin I, flavodoxin II and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner, i.e. reaction of EC 1.18.2.1. Flavodoxin I and flavodoxin II behave similarly with respect to FNR, with affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin. Flavodoxin I and flavodoxin II can obtain electrons from reduced Fd at rates that are comparable to those obtained with reduced FNR
Products: -
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?
additional information
?
-
-
Substrates: substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein
Products: -
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?
additional information
?
-
-
Substrates: the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples
Products: -
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?
additional information
?
-
Substrates: Escherichia coli FNR (EcFPR) contains 0.99 NADP+/FNR (mol/mol). Escherichia coli FPR (EcFPR) contains tightly bound NADP+, which does not occur in plastidic type FNRs. Escherichia coli FPR (EcFPR) can exchange reduction equivalents with both ferredoxin and flavodoxin
Products: -
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?
additional information
?
-
Escherichia coli B / ATCC 11303
-
Substrates: substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein
Products: -
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?
additional information
?
-
-
Substrates: the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples
Products: -
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?
additional information
?
-
Substrates: Escherichia coli FNR (EcFPR) contains 0.99 NADP+/FNR (mol/mol). Escherichia coli FPR (EcFPR) contains tightly bound NADP+, which does not occur in plastidic type FNRs. Escherichia coli FPR (EcFPR) can exchange reduction equivalents with both ferredoxin and flavodoxin
Products: -
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?
additional information
?
-
Substrates: no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
Products: -
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?
additional information
?
-
Substrates: no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
Products: -
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?
additional information
?
-
A0A7T5QNX4
Substrates: Pectobacterium carotovorum FNR (PcFPR) contains 0.65 NADP+/FNR (mol/mol)
Products: -
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?
additional information
?
-
Substrates: enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
Products: -
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?
additional information
?
-
-
Substrates: enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
Products: -
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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
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
Substrates: -
Products: -
Products: -
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme reduces flavodoxin I, flavodoxin II and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner, i.e. reaction of EC 1.18.2.1. Flavodoxin I and flavodoxin II behave similarly with respect to FNR, with affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin. Flavodoxin I and flavodoxin II can obtain electrons from reduced Fd at rates that are comparable to those obtained with reduced FNR
Products: -
Products: -
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
A0A7T5QNX4
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
reduction of the FAD moiety of phenylglyoxal-modified FNR by laser-generated 5-deazariboflavin semiquinone occurs with a second-order rate constant 2.5fold smaller than that obtained for reduction of native FNR
FAD
-
oxidized FLDR has flavin absorbance maxima at 456 nm and 400 nm, with a shoulder on the longer wavelength band at 483 nm
FAD
-
FAD-binding domain comparison of FNR1 and FNR2, structure-function analysis
FAD
prosthetic group. Both plastidic and bacterial FNRs fold in two domains. The N-terminal and C-terminal domains are responsible for the binding of the prosthetic group FAD and the substrate NADP(H), respectively. The folded FAD in FPRs is stabilized by the stacking of its adenosine to an aromatic residue found in a C-terminal tail present in FPRs but absent in FNRs
FAD
A0A7T5QNX4
prosthetic group. Both plastidic and bacterial FNRs fold in two domains. The N-terminal and C-terminal domains are responsible for the binding of the prosthetic group FAD and the substrate NADP(H), respectively. The folded FAD in FPRs is stabilized by the stacking of its adenosine to an aromatic residue found in a C-terminal tail present in FPRs but absent in FNRs
FAD
prosthetic group. Both plastidic and bacterial FNRs fold in two domains. The N-terminal and C-terminal domains are responsible for the binding of the prosthetic group FAD and the substrate NADP(H), respectively. The folded FAD in FPRs is stabilized by the stacking of its adenosine to an aromatic residue found in a C-terminal tail present in FPRs but absent in FNRs
NADP+
Kd value 0.222 mM, coenzyme docking occurrs through the 2'-P-AMP moiety
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
NADP+ produces an inhibition on EcFPR as the wild-type enzyme is 10times more catalytically efficient when the oxidized nucleotide generated is depleted from the reaction medium. This inhibition is not observed with the different EcFPR mutant variant. Residues R144 and R184 are involved in the inhibition site
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavodoxin
cytochrome c reductase activity of FPR is stimulated three times by the addition of flavodoxin
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
ferricytochrome c
presence of flavodoxin, pH 8.0, temperature not specified in the publication
0.009
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.02
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.039
NADPH
mutant A266Y/Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.043
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.08
NADPH
substrate ferricyanide, pH 8.0, temperature not specified in the publication
0.085
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.0044
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.0047
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.025
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
0.008
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.013
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
0.06
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.00074
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.0027
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.061
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
additional information
additional information
kinetics for NADPH-ferricyanide diaphorase activity of wild-type and mutant enzymes
-
additional information
additional information
A0A7T5QNX4
kinetics for NADPH-ferricyanide diaphorase activity
-
additional information
additional information
kinetics for NADPH-ferricyanide diaphorase activity
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
ferricytochrome c
presence of flavodoxin, pH 8.0, temperature not specified in the publication
1
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
7
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
7.2
NADPH
substrate ferricyanide, pH 8.0, temperature not specified in the publication
8
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
12
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
20
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.04
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.122
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
46.3
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
0.048
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.7
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
152.1
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
0.049
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
0.133
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
1.67
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.09
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
25.96
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
1852
reduced flavodoxin 1
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
6
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
11.67
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
11700
reduced flavodoxin 2
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
27.38
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR2
-
49.26
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
66.22
reduced flavodoxin-like protein NrdI
-
pH 7.5, temperature not specified in the publication, recombinant FNR1
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
Uniprot
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
SwissProt
brenda
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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
evolution
malfunction
enzyme deletion produces bacteria that are highly sensitive to oxidative stress
metabolism
Escherichia coli FPR (EcFPR) can exchange reduction equivalents with both ferredoxin and flavodoxin. The direction of the reaction in bacteria is optimized to favor the consumption of NADPH. The enzyme participates in several metabolic pathways. Bacteria need to finely regulate NADP(H) pool homeostasis to generate an appropriate stress response. This regulatory function is carried out with the direct participation of FPR
physiological function
additional information
evolution
-
ferredoxin/flavodoxin NADP+ oxidoreductases, FNRs, can be separated into two main families, plant-type FNRs and glutathione reductase (GR)-like FNRs, which are structurally and phylogenetically unrelated. Bacillus cereus FNRs, FNR1-3, belong to the dimeric thioredoxin reductase (TrxR)-like subfamily of the GR-like FNRs. Bioinformatic analysis shows that the TrxR-like FNRs can actually be divided into two groups, one group where the FAD-stacking residue has aromatic character and another group where it is valine
evolution
ferredoxin-NADP+ reductases (FNRs) constitute a family of monomeric hydrophilic proteins that contain noncovalently bound FAD as a prosthetic group. These enzymes are widely distributed among organisms and are involved in the electron transfer of biologically important processes. Ferredoxin-NADP+ reductases (FNRs) are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. A difference between FNRs and FPRs also occurs at the active site. The FAD isoalloxazine ring stacks between two aromatic residues, being on the reface a conserved C-terminal tyrosine in plastidic FNRs. Subclass II FPRs conserve this aromatic residue, but subclass I members lack it. Subclass I FPRs are subdivided into two groups: subclass IA and subclass IB. The main structural differences between these subclasses are located in the C-terminal region. While enzymes from subclass IA have a conserved lysine, the subclass IB FPRs have a glutamate or an aspartate at the equivalent position and a more extended C-terminal region. Consequently, subclass IA is defined by the C-terminal sequence VEK and the subclass IB by the sequence (V/A)G(E/D)G(I/V). FPRs show differential NADP+ binding mode and catalytic mechanism from the ones previously described for the plastidic type FNRs
evolution
A0A7T5QNX4
ferredoxin-NADP+ reductases (FNRs) constitute a family of monomeric hydrophilic proteins that contain noncovalently bound FAD as a prosthetic group. These enzymes are widely distributed among organisms and are involved in the electron transfer of biologically important processes. Ferredoxin-NADP+ reductases (FNRs) are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. A difference between FNRs and FPRs also occurs at the active site. The FAD isoalloxazine ring stacks between two aromatic residues, being on the reface a conserved C-terminal tyrosine in plastidic FNRs. Subclass II FPRs conserve this aromatic residue, but subclass I members lack it. Subclass I FPRs are subdivided into two groups: subclass IA and subclass IB. The main structural differences between these subclasses are located in the C-terminal region. While enzymes from subclass IA have a conserved lysine, the subclass IB FPRs have a glutamate or an aspartate at the equivalent position and a more extended C-terminal region. Consequently, subclass IA is defined by the C-terminal sequence VEK and the subclass IB by the sequence (V/A)G(E/D)G(I/V). FPRs show differential NADP+ binding mode and catalytic mechanism from the ones previously described for the plastidic type FNRs
evolution
ferredoxin-NADP+ reductases (FNRs) constitute a family of monomeric hydrophilic proteins that contain noncovalently bound FAD as a prosthetic group. These enzymes are widely distributed among organisms and are involved in the electron transfer of biologically important processes. Ferredoxin-NADP+ reductases (FNRs) are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. A difference between FNRs and FPRs also occurs at the active site. The FAD isoalloxazine ring stacks between two aromatic residues, being on the reface a conserved C-terminal tyrosine in plastidic FNRs. Subclass II FPRs conserve this aromatic residue, but subclass I members lack it. Subclass I FPRs are subdivided into two groups: subclass IA and subclass IB. The main structural differences between these subclasses are located in the C-terminal region. While enzymes from subclass IA have a conserved lysine, the subclass IB FPRs have a glutamate or an aspartate at the equivalent position and a more extended C-terminal region. Consequently, subclass IA is defined by the C-terminal sequence VEK and the subclass IB by the sequence (V/A)G(E/D)G(I/V). FPRs show differential NADP+ binding mode and catalytic mechanism from the ones previously described for the plastidic type FNRs
evolution
-
ferredoxin-NADP+ reductases (FNRs) constitute a family of monomeric hydrophilic proteins that contain noncovalently bound FAD as a prosthetic group. These enzymes are widely distributed among organisms and are involved in the electron transfer of biologically important processes. Ferredoxin-NADP+ reductases (FNRs) are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. A difference between FNRs and FPRs also occurs at the active site. The FAD isoalloxazine ring stacks between two aromatic residues, being on the reface a conserved C-terminal tyrosine in plastidic FNRs. Subclass II FPRs conserve this aromatic residue, but subclass I members lack it. Subclass I FPRs are subdivided into two groups: subclass IA and subclass IB. The main structural differences between these subclasses are located in the C-terminal region. While enzymes from subclass IA have a conserved lysine, the subclass IB FPRs have a glutamate or an aspartate at the equivalent position and a more extended C-terminal region. Consequently, subclass IA is defined by the C-terminal sequence VEK and the subclass IB by the sequence (V/A)G(E/D)G(I/V). FPRs show differential NADP+ binding mode and catalytic mechanism from the ones previously described for the plastidic type FNRs
-
physiological function
insertion mutants lacking a functional enzyme do not require methionine and grow well anaerobically, but they show increased sensitivity to paraquat
physiological function
Escherichia coli cells deficient in the soxRS-induced ferredoxin (flavodoxin)-NADP(H) reductase FPR, display abnormal sensitivity to methyl viologen. Neither bacteriostatic effects nor inactivation of oxidant-sensitive hydrolyases can be detected in mutant cells exposed to methyl viologen. FPR inactivation does not affect the methyl viologen-driven soxRS response, FPR overexpression leads to enhanced stimulation of the regulon, with concomitant oxidation of the NADPH pool. Accumulation of a site-directed FPR mutant that uses NAD(H) instead of NADP(H) has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
physiological function
flavodoxin, flavodoxin reductase and NADPH function during the activation of the anaerobic ribonucleotide reductase
physiological function
ferredoxin-NADP+ reductases (FNRs) are ubiquitous flavoenzymes involved in redox metabolisms. FNRs catalyze the reversible electron transfer between NADP(H) and ferredoxin (EC 1.18.1.2) or flavodoxin (EC 1.19.1.1). They are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. The plastidic FNRs show turnover numbers between 20 and 100 times higher than bacterial enzymes and these differences have been related to their physiological functions. Bacteria need to finely regulate NADP(H) pool homeostasis to generate an appropriate stress response. This regulatory function is carried out with the direct participation of FPR
physiological function
A0A7T5QNX4
ferredoxin-NADP+ reductases (FNRs) are ubiquitous flavoenzymes involved in redox metabolisms. FNRs catalyze the reversible electron transfer between NADP(H) and ferredoxin (EC 1.18.1.2) or flavodoxin (EC 1.19.1.1). They are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. The plastidic FNRs show turnover numbers between 20 and 100 times higher than bacterial enzymes and these differences have been related to their physiological functions
physiological function
ferredoxin-NADP+ reductases (FNRs) are ubiquitous flavoenzymes involved in redox metabolisms. FNRs catalyze the reversible electron transfer between NADP(H) and ferredoxin (EC 1.18.1.2) or flavodoxin (EC 1.19.1.1). They are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. The plastidic FNRs show turnover numbers between 20 and 100 times higher than bacterial enzymes and these differences have been related to their physiological functions
physiological function
-
ferredoxin-NADP+ reductases (FNRs) are ubiquitous flavoenzymes involved in redox metabolisms. FNRs catalyze the reversible electron transfer between NADP(H) and ferredoxin (EC 1.18.1.2) or flavodoxin (EC 1.19.1.1). They are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. The plastidic FNRs show turnover numbers between 20 and 100 times higher than bacterial enzymes and these differences have been related to their physiological functions
-
additional information
-
interaction analysis of two flavodoxins (Fld1-2), one flavodoxin-like protein (NrdI), and three different thioredoxin reductase (TrxR)-like FNRs (FNR1-3), steady-state kinetics, overview. A large-scale conformational rearrangement takes place during the FNR catalytic cycle to allow for the binding and reduction of the Fld and, subsequently, the re-reduction of the FNR by NADPH. The FNR2-Fld2 electron transfer pair is particularly efficient, and redox potential measurements also indicate that this is the most favorable electron donor/acceptor pair
additional information
-
interaction analysis of two flavodoxins (Fld1-2), one flavodoxin-like protein (NrdI), and three different thioredoxin reductase (TrxR)-like FNRs (FNR1-3), steady-state kinetics, overview
additional information
the three-dimensional structure showed that the NADP+ molecule interacts with three arginines, R144, R174, and R184. These residues could be responsible for generating a structured site with a very high affinity for NADP+. These arginine residues are conserved in other FPRs of different subclasses, but not in the plastidic type enzymes. Comparisons of the nucleotide binding site sequence of FNRs, overview
additional information
A0A7T5QNX4
the three-dimensional structure showed that the NADP+ molecule interacts with three arginines. These residues could be responsible for generating a structured site with a very high affinity for NADP+. These arginine residues are conserved in other FPRs of different subclasses, but not in the plastidic type enzymes. Comparisons of the nucleotide binding site sequence of FNRs, overview
additional information
the three-dimensional structure showed that the NADP+ molecule interacts with three arginines. These residues could be responsible for generating a structured site with a very high affinity for NADP+. These arginine residues are conserved in other FPRs of different subclasses, but not in the plastidic type enzymes. Comparisons of the nucleotide binding site sequence of FNRs, overview
Show AA Sequence and Transmembrane Helices (1261 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
monomer
-
1 * 27620, calculated, 1 * 27 648, electrospray mass spectroscopy
-
additional information
the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
additional information
the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
additional information
-
the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme FNR1 crystallizes in a closed conformation, X-ray diffraction structure determination and analysis at 2.5 A resolution. The FNR1 sequence is homology modeled with the FNR2 structure (PDB ID 6gas) used as template. The FAD-binding domain of the original FNR1 structure (PDB ID 6gar) is aligned to the modeled FNR1 structure, and the FAD groups and the C-terminal helices from the original structure are added to the homology modeled FNR1
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enzyme FNR2 crystallizes in an open conformation, NADP+ and FNR2 are mixed to final NADP+ concentration of 5 mM and FNR2 concentration 16 mg/ml, mixing in a 1:1 ratio with 400 nl reservoir solution, containing 0.1 M sodium chloride, 0.02 M Tris pH 7.0, 7.7% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.4 A resolution. The FNR1 sequence is homology modeled with the FNR2 structure (PDB ID 6gas) used as template. The FAD-binding domain of the original FNR1 structure (PDB ID 6gar) is aligned to the modeled FNR1 structure, and the FAD groups and the C-terminal helices from the original structure are added to the homology modeled FNR1
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structure to 2.5 A resolution, orthorhombic space group P21212, with unit-cell parameters a = 57.2, b = 164.3, c = 95.0 A, containing two protein molecules in the asymmetric unit
molecular modelling indicates that movement of the C-terminal tryptophan (W248) is necessary to permit close approach of the nicotinamide ring of NADPH to the flavin. Residues R174 and R184 are located close to the adenosine ribose 2'-phosphate group, and R144 is likely to interact with the nicotinamide ribose 5'-phosphate group
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a multiscale modelling approach for analysis of the electron transfer process in complexes of the enzyme with both ferredoxin and flavodoxin, reactions of EC 1.19.1.1 and EC1.18.1.2, respectively. The electron transfer in FNR/ferredoxin proceedes through a bridge-mediated mechanism in a dominant protein-protein complex, where transfer of the electron is facilitated by ferredoxin loop-residues 40-49. In FNR/flavodoxin, a direct transfer between redox cofactors is observed and less complex specificity than in ferredoxin
in complex with 2'-phospho-AMP and NADP+. In the complexes obtained, the nucleotides bind exclusively through the adenosine moiety. The adenosine moiety binds into a cavity formed by residues of conserved segments, i.e residues 128 to 130, residues 158 to 163, residues 193 to 205, and residues 233 to 240. The adenosine binding site is essentially formed by residues R158, R195 and R203, which stabilise the nucleotide
to 2.17 A resolution, tetragonal space group P41212, with unit-cell parameters a = b = 66.49, c = 121.32 A
no perturbation of the 31P-NMR resonances assigned to the FAD moiety of FNR or the FMN and phosphodiester moieties of Azotobacter flavodoxin are observed on complexation of Azotobacter flavodoxin and Spinacia oleracea FNR. Reduction of FMN to its semiquinone form results in extensive line-broadening of the FMN resonance. The FAD resonances of the FNR-flavodoxin complex are unaffected by FMN semiquinone formation. The distance from the FMN phosphate to the flavin ring is altered on binding the flavodoxin to FNR
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y50G
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50S
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50W
mutation results in a blue shift of the FAD transition bands, with quenching of fluorescence emission. Mutant displays decreased thermal stability
Y50G
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
Y50S
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
R144A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
R144P
site-directed mutagenesis, the catalytic efficency of the mutant is reduced one-fold compared to wild-type enzyme
R144P/R148Y
site-directed mutagenesis, the catalytic efficency of the mutant is reduced three-fold compared to wild-type enzyme
R148Y
site-directed mutagenesis, the catalytic efficency of the mutant is reduced two-fold compared to wild-type enzyme
R174A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
R184A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
Y308S
mutant uses NAD(H) instead of NADP(H), expression of the mutant has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
R144A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R174A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R184A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R144P
-
site-directed mutagenesis, the catalytic efficency of the mutant is reduced one-fold compared to wild-type enzyme
-
R148Y
-
site-directed mutagenesis, the catalytic efficency of the mutant is reduced two-fold compared to wild-type enzyme
-
Y308F
about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin
Y308S
nearly inactive mutant with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y308W
about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin
Y303F
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
Y303S
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y303F
-
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
-
Y303S
-
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
-
A266Y
mutant does not allow formation of active charge-transfer complexes, probably due to restraints of C-terminus pliability. Mutant displays higher affinity for NADP+ than wild-type
A266y/Del267-272
deletion/mutation emulates the structure present in plastidic versions of the protein. It does not modify the general geometry of FAD itself, but increases exposure of the flavin to the solvent, prevents a productive geometry of FAD:NADP(H) complex and decreases the protein thermal stability. Mutant displays higher affinity for NADP+ than wild-type
Del267-272
deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
reduced FNR is subject to inactivation due to unfolding of the protein and dissociation of the FADH2 cofactor
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme
-
FNR reduced in the presence of NADPH is slowly inactivated under all conditions. Reactivity towards flavodoxin is lost most rapidly (kinact of 0.031 per min) with less than 10% of the original activity remaining after 30 min, reactivity towards ferredoxin is not as rapidly affected (kinact of 0.0065 per min) with 80% of the original activity remaining after 30 min
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli
recpmbinant protein. FLDR is bright yellow in its oxidized form and it is converted to a neutral blue semiquinone by the addition of one reducing equivalent
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
FNR2, sequence comparisons and phylogenetic analysis, recombinant expression
-
gene fpr, recombinant expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wan, J.T.; Jarrett, J.T.
Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli
Arch. Biochem. Biophys.
406
116-126
2002
Escherichia coli (P28861)
brenda
Nogues, I.; Tejero, J.; Hurley, J.K.; Paladini, D.; Frago, S.; Tollin, G.; Mayhew, S.G.; Gomez-Moreno, C.; Ceccarelli, E.A.; Carrillo, N.; Medina, M.
Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin
Biochemistry
43
6127-6137
2004
Lathyrus oleraceus (P10933), Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
brenda
Jarrett, J.T.; Wan, J.T.
Thermal inactivation of reduced ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli
FEBS Lett.
529
237-242
2002
Escherichia coli
brenda
Bittel, C.; Tabares, L.C.; Armesto, M.; Carrillo, N.; Cortez, N.
The oxidant-responsive diaphorase of Rhodobacter capsulatus is a ferredoxin (flavodoxin)-NADP(H) reductase
FEBS Lett.
553
408-412
2003
Rhodobacter capsulatus (Q9L6V3)
brenda
Crain, A.V.; Broderick, J.B.
Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme
Biochim. Biophys. Acta
1834
2512-2519
2013
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Perez-Dorado, I.; Bortolotti, A.; Cortez, N.; Hermoso, J.A.
Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus
Acta Crystallogr. Sect. F
64
375-377
2008
Rhodobacter capsulatus (D5ATP7), Rhodobacter capsulatus ATCC BAA-309 (D5ATP7)
brenda
Skramo, S.; Hersleth, H.P.; Hammerstad, M.; Andersson, K.K.; Rohr, A.K.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus
Acta Crystallogr. Sect. F
70
777-780
2014
Bacillus cereus (Q81IK1), Bacillus cereus, Bacillus cereus DSM 31 (Q81IK1)
brenda
Bianchi, V.; Eliasson, R.; Fontecave, M.; Mulliez, E.; Hoover, D.M.; Matthews, R.G.; Reichard, P.
Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase
Biochem. Biophys. Res. Commun.
197
792-797
1993
Escherichia coli (P28861)
brenda
Leadbeater, C.; McIver, L.; Campopiano, D.; Webster, S.; Baxter, R.; Kelly, S.; Price, N.; Lysek, D.; Noble, M.; Chapman, S.; Munro, A.
Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase
Biochem. J.
352
257-266
2000
Escherichia coli, Escherichia coli HMS174
brenda
Bortolotti, A.; Perez-Dorado, I.; Goni, G.; Medina, M.; Hermoso, J.A.; Carrillo, N.; Cortez, N.
Coenzyme binding and hydride transfer in Rhodobacter capsulatus ferredoxin/flavodoxin NADP(H) oxidoreductase
Biochim. Biophys. Acta
1794
199-210
2009
Rhodobacter capsulatus (Q9L6V3)
brenda
Bortolotti, A.; Sanchez-Azqueta, A.; Maya, C.M.; Velazquez-Campoy, A.; Hermoso, J.A.; Medina, M.; Cortez, N.
The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme
Biochim. Biophys. Acta
1837
33-43
2014
Rhodobacter capsulatus (Q9L6V3)
brenda
Saen-Oon, S.; Cabeza De Vaca, I.; Masone, D.; Medina, M.; Guallar, V.
A theoretical multiscale treatment of protein-protein electron transfer: The ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems
Biochim. Biophys. Acta
1847
1530-1538
2015
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
brenda
Bonants, P.J.; Mller, F.; Vervoort, J.; Edmondson, D.E.
A 31Pnuclear-magneticresonance study of NADPH-cytochrome-P-450 reductase and of the Azotobacter flavodoxin/ferredoxin-NADP+ reductase complex
Eur. J. Biochem.
190
531-537
1990
Spinacia oleracea (P00455)
brenda
Medina, M.; Gomez-Moreno, C.; Tollin, G.
Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP+ reductase on the kinetics of interprotein electron transfer reactions
Eur. J. Biochem.
210
577-583
1992
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
brenda
McIver, L.; Leadbeater, C.; Campopiano, D.J.; Baxter, R.L.; Daff, S.N.; Chapman, S.K.; Munro, A.W.
Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli
Eur. J. Biochem.
257
577-585
1998
Escherichia coli, Escherichia coli HMS174
brenda
Bianchi, V.; Haggard-Ljungquist, E.; Pontis, E.; Reichard, P.
Interruption of the ferredoxin (flavodoxin) NADP+ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat
J. Bacteriol.
177
4528-4531
1995
Escherichia coli (P28861)
brenda
Krapp, A.R.; Rodriguez, R.E.; Poli, H.O.; Paladini, D.H.; Palatnik, J.F.; Carrillo, N.
The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli
J. Bacteriol.
184
1474-1480
2002
Escherichia coli (P28861)
brenda
Seo, D.; Naito, H.; Nishimura, E.; Sakurai, T.
Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH
Photosynth. Res.
125
321-328
2015
Bacillus subtilis (O05268), Bacillus subtilis 168 (O05268)
brenda
Gudim, I.; Hammerstad, M.; Lofstad, M.; Hersleth, H.P.
The characterization of different flavodoxin reductase-flavodoxin (FNR-Fld) interactions reveals an efficient FNR-Fld redox pair and identifies a novel FNR subclass
Biochemistry
57
5427-5436
2018
Bacillus cereus
brenda
Monchietti, P.; Lopez Rivero, A.S.; Ceccarelli, E.A.; Catalano-Dupuy, D.L.
A new catalytic mechanism of bacterial ferredoxin-NADP+ reductases due to a particular NADP+ binding mode
Protein Sci.
30
2106-2120
2021
Brucella abortus (Q2YPI0), Brucella abortus 2308 (Q2YPI0), Escherichia coli (P28861), Escherichia coli K12 (P28861), Pectobacterium carotovorum (A0A7T5QNX4)
brenda
EXTERNAL LINKS (specific for EC-Number 1.19.1.1)
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