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
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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
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RECOMMENDED NAME
GeneOntology No.
ferredoxin-NADP+ reductase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Photosynthesis
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photosynthesis light reactions
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photosynthesis
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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
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 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
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diaphorase activity, no activity with NADH
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?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
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?, r
additional information
?
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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 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
O05268
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r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
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?
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
0.57
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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below 0.1 mM, oxidized ferredoxin with NADH, pH 7.0, 24C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
NADH
Bacillus subtilis
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ferredoxin reduction, pH 7.0, 24C
22.7 - 35.4
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
dimer
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2 * 40000, SDS-PAGE
additional information
structure, primary sequence and oligomeric conformation, comparisons, overview
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
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
additional information
site-directed mutagenesis of NADPH-specific BsFNR to replace Arg186, Asp187, Arg190, and His324 with the residues occurring in NADH/NADPH-bispecific Chlorobium tepidum FNR