Information on EC 1.7.7.2 - ferredoxin-nitrate reductase

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

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EC NUMBER
COMMENTARY hide
1.7.7.2
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RECOMMENDED NAME
GeneOntology No.
ferredoxin-nitrate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nitrite + H2O + 2 oxidized ferredoxin = nitrate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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-
nitrate reduction VI (assimilatory)
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Nitrogen metabolism
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nitrate assimilation
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-
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SYSTEMATIC NAME
IUBMB Comments
nitrite:ferredoxin oxidoreductase
A molybdenum-iron-sulfur protein.
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CAS REGISTRY NUMBER
COMMENTARY hide
60382-69-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 7119
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-
Manually annotated by BRENDA team
strain ATCC 29413
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-
Manually annotated by BRENDA team
strains 7101 and 7601
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-
Manually annotated by BRENDA team
heterocystous nitrogen-fixing cyanobacterial strains
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-
Manually annotated by BRENDA team
strain 7119
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-
Manually annotated by BRENDA team
strain N1, phototrophic, purple sulfur bacterium
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-
Manually annotated by BRENDA team
strain N1, phototrophic, purple sulfur bacterium
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-
Manually annotated by BRENDA team
strain 1829
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-
Manually annotated by BRENDA team
strain 1829
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain CU 1462/7
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-
Manually annotated by BRENDA team
strain CU 1462/7
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-
Manually annotated by BRENDA team
formerly known as Anacystis nidulans
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-
Manually annotated by BRENDA team
strain WH 8102
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-
Manually annotated by BRENDA team
strain 6803, unicellular cyanobacterium
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-
Manually annotated by BRENDA team
Thermosynechococcus sp.
strain BP-1
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-
Manually annotated by BRENDA team
strain BP-1
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-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chlorate + reduced methylviologen
chlorite + H2O + oxidized methylviologen
show the reaction diagram
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6% of kcat with nitrate
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-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
nitrate + reduced flavodoxin
nitrite + H2O + oxidized flavodoxin
show the reaction diagram
nitrate + reduced flavodoxin
nitrite + oxidized flavodoxin + H2O
show the reaction diagram
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flavodoxin can physiologically substitute for ferredoxin under conditions of iron starvation
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nitrate + reduced methyl viologen
nitrite + H2O + oxidized methyl viologen
show the reaction diagram
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
nitrate + reduced methylviologen
nitrite + H2O + oxidized methylviologen
show the reaction diagram
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-
-
-
?
selenate + reduced methylviologen
selenite + H2O + oxidized methylviologen
show the reaction diagram
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1% of kcat with nitrate
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-
?
additional information
?
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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
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
nitrate + reduced flavodoxin
nitrite + oxidized flavodoxin + H2O
show the reaction diagram
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flavodoxin can physiologically substitute for ferredoxin under conditions of iron starvation
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
heme c
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enzyme contains 1.5 heme molecules of the c-type
iron-sulfur centre
molybdenum cofactor
molybdopterin
additional information
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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stimulates activity about 30%
Fe2+
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stimulates activity about 50%
iron-sulfur centre
Mg2+
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stimulates activity about 30%
Mn2+
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stimulates activity about 50%, stimulates reaction rate and level of nitrite formation
Molybdenum
NaCl
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activity depends on salt concentration
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonia
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after initial slight stimulation rapid and complete inhibition, promotes conversion of ferredoxin-nitrate reductase into its reduced inactive form, metabolic interconversion
azide
cyanide
Dithionite
FAD
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photoactivated FAD, irreversible inactivation
KCl
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inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
light
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light- and oxygen-dependent inactivation of enzyme activity in absence but not in presence of any added nitrogen source, inactivation may result from an oxidative modification of enzyme, assay in cell suspension
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MgSO4
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inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
N-acetylsuccinimide
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115fold excess, loss of more than 80% and 5-10% loss of ferredoxin-dependent and methylviologen dependent activity after 1 h, respectively
NaCl
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more than 80% inhibition above 200 mM, inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
oxygen
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light- and oxygen-dependent inactivation of enzyme activity in absence but not in presence of any added nitrogen source, inactivation may result from an oxidative modification of enzyme, assay in cell suspension
p-hydroxymercuribenzoate
Phenylglyoxal
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76fold excess, approx. 60% and 20% loss of ferredoxin dependent and methylviologen dependent activity after 2 h, respectively
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cyanate
additional information
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
Ferredoxin
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spinach ferredoxin
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0.05 - 2.1
nitrate
0.013 - 0.038
reduced ferredoxin
0.066 - 2.5
reduced methyl viologen
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80 - 1090
nitrate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
azide
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25°C, pH 8.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.2
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in situ assay, cells grown on media containing nitrate
305
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ferredoxin-linked activity
1020
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methyl viologen-linked activity
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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anaerobic assay, methyl viologen- and ferredoxin-linked activity
9.5 - 10.5
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reduced methyl viologen as electron donor
10.2
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aerobic assay, methyl viologen-linked activity
10.5
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dithionite-reduced methyl viologen as electron donor
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.2
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at pH 7.3 and 9.2: 50% of activity maximum, aerobic assay, methyl viologen-linked and ferredoxin-linked activity
8.3 - 9.8
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at pH 8.3 and 9.8: about 50% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
for NaCl concentrations of 1.3 and 0.9 M
80
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for NaCl concentrations of 3.1 and 2.2 M
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme functions in the soluble state in the cytoplasm
Manually annotated by BRENDA team
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tightly bound to chlorophyll-containing membrane fractions
Manually annotated by BRENDA team
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recombinant enzyme activity is found exclusively in the soluble fraction
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Manually annotated by BRENDA team
additional information
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activity remains associated with photosynthetic subcellular particles
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Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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1 * 105000 + 1 * 50000, SDS-PAGE
78000
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x * 78000, SDS-PAGE
83000
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1 * 83000, SDS-PAGE
90000
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ultracentrifugation
100000
105000
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1 * 105000 + 1 * 50000, SDS-PAGE
132000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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5 min, crude extract, stable
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low ionic strength, 70 h, 0.002 mg protein/ml, 10 mM phosphate buffer or 50 mM Tris-HCl buffer, pH 7.5, unstable
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NaCl stabilizes, after 43 h, with 2.7 M, 2.1 M or 0.9 M NaCl: 95% loss of activity, after 90 h, with 4.3 M NaCl: completely stable
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
reversible inactivation of ferredoxin-linked activity by exposure of dithionite solution of the enzyme to air, but no effect on methyl viologen-linked activity
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440443
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol, several months, no loss of activity
-20°C, in 50 mM Tris-HCl buffer, pH 7.5, 0.5 M NaCl, 1 mM EDTA, 1 month, no loss of activity
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4°C, 50 mM phosphate buffer, pH 7, 20% glycerol, 2 weeks, no loss of activity
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4°C, several weeks, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
177fold purification
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185fold partial purification
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19000fold purification
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partial purification
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purified from a few cyanobacterial strains
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recombinant enzyme
recombinant His-tagged nitrate reductase, Ni2+-affinity column
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recombinant nitrate reductase
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of His-tagged nitrate reductase in Escherichia coli
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expression of native and His-tagged nitrate reductase in Escherichia coli
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narB structural gene for nitrate reductase is cloned and expressed in Escherichia coli as a 76 kDa polypeptide with 729 amino acids
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strain 7120: gene encoding nitrate reductase is cloned and its complete amino acid sequence deduced
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C12A
no actiivty, no iron-sulfur cluster
C16S
1.9% of wild type activity with ferredoxin, no iron-sulfur cluster
C56A
no activity, no iron-sulfur cluster
C56S
70% of wild type activity with ferredoxin, contains an iron-sulfur cluster
C9A
no activity, no iron-sulfur cluster
C9H
no narB expression
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LINKS TO OTHER DATABASES (specific for EC-Number 1.7.7.2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)