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Information on EC 1.19.1.1 - flavodoxin-NADP+ reductase and Organism(s) Escherichia coli and UniProt Accession P28861
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1.19.1.1 flavodoxin-NADP+ reductaseIUBMB 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.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
Bc_0385, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin/flavodoxin-NADP(H) oxidoreductase, FLDR, FNR, FPR, PETH, YumC, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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.
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 flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
?
additional information
?
-
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
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-
?
additional information
?
-
-
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
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-
?
additional information
?
-
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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
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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 flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
?
additional information
?
-
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
oxidized FLDR has flavin absorbance maxima at 456 nm and 400 nm, with a shoulder on the longer wavelength band at 483 nm
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
insertion mutants lacking a functional enzyme do not require methionine and grow well anaerobically, but they show increased sensitivity to paraquat
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
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)
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
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
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)
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
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
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)
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