Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Bacillus subtilis and UniProt Accession O05268

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Bacillus subtilis
UNIPROT: O05268


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea


The taxonomic range for the selected organisms is: Bacillus subtilis

EC NUMBER
COMMENTARY hide
1.18.1.2
-
RECOMMENDED NAME
GeneOntology No.
ferredoxin-NADP+ reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
a hydride transfer reaction with NAD(P)H and two separate one-electron transfer reactions with ferredoxin are generally involved in te reaction process
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photosynthesis light reactions
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photosynthesis
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Photosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NADP+ oxidoreductase
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.
CAS REGISTRY NUMBER
COMMENTARY hide
56367-57-8
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9029-33-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the flavoprotein superfamily
physiological function
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FNR mediates the redox reaction between NADP+/NADPH and ferredoxin, providing redox equivalents in cell-material synthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
show the reaction diagram
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
diaphorase activity, no activity with NADH
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-
?
reduced cytochrome c + NADPH + H+
oxidized cytochrome c + NADPH
show the reaction diagram
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?, r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme also shows NAD(P)H oxidase activity, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
show the reaction diagram
O05268
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-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
O05268
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-
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r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
O05268
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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reverse reaction: preferred cofactor, poor activity with NADH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019 - 0.0197
NADPH
0.57
NADPH
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2,6-dichlorophenolindophenol reduction, pH 7.0, 24C
0.54
oxidized ferredoxin
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with NADPH, pH 7.0, 24C
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.2 - 1012
NADPH
0.4
NADH
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ferredoxin reduction, pH 7.0, 24C
22.7 - 35.4
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8526 - 51370
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33.8
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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2 * 40000, SDS-PAGE
94000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, SDS-PAGE
monomer
1 * 40000, recombinant mutant enzymes, SDS-PAGE
dimer
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2 * 40000, SDS-PAGE
homodimer
2 * 40000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FNR in complex with NADP+, two different crystal forms, mixing of 0.001 ml of 10 mg/ml protein and 2.5 mM NADP+ with 0.001 ml of reservoir solution containing 0.1 M HEPES buffer, pH 7.5, 30% 1,2-propanediol, and 20% PEG 400 for form I, and 20% PEG 3350, 0.2 M sodium fluoride, and 5% trehalose for form II, 20C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, respetively, molecular replacement
purified recombinant FNR in complex with NADP+ in two different forms, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl pH 8.0, 200 mM NaCl, and 2.5 mM NADP+, is mixed with 0.001 ml reservoir solution, 20C. The reservoir solutions consist of 0.1 M HEPES buffer pH 7.5, 30% 1,2-propanediol, 20% PEG 400 for form I, and of 20% PEG 3350, 0.2 M sodium fluoride and 5% trehalose for form II. X-ray diffraction structure determination and analysis at 1.8 and 1.9 A resolution, respectively, molecular replacement, modelling
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from cell extract 86fold to homogeneity by several chromatographic steps
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H324F
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
H324S
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R186G
site-directed mutagenesis, replacement of Arg186 with glycine leads to drastically reduced amounts of recombinant protein
R186G/D187H
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R186G/D187H/R190Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R190Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
Y50G
the mutation decreases thermal stability compared to the wild type enzyme
Y50S
the mutation decreases thermal stability compared to the wild type enzyme
Y50W
the mutation decreases thermal stability compared to the wild type enzyme, The mutant retains approximately 20% of wild type reactivity
additional information