Information on EC 1.7.7.2 - ferredoxin-nitrate reductase

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

EC NUMBER
COMMENTARY
1.7.7.2
-
RECOMMENDED NAME
GeneOntology No.
ferredoxin-nitrate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nitrite + H2O + 2 oxidized ferredoxin = nitrate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
nitrate reduction VI (assimilatory)
-
Nitrogen metabolism
-
SYSTEMATIC NAME
IUBMB Comments
nitrite:ferredoxin oxidoreductase
A molybdenum-iron-sulfur protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
assimilatory ferredoxin-nitrate reductase
-
-
-
-
Assimilatory nitrate reductase
-
-
-
-
Assimilatory nitrate reductase
-
-
narB
P39458
-
narB
Synechococcus sp. WH
-
-
-
narB
Synechocystis sp., Thermosynechococcus sp.
-
-
narB
Thermosynechococcus sp. BP-1
-
-
-
nitrate (ferredoxin) reductase
-
-
-
-
nitrate reductase
Synechococcus sp. WH
-
-
-
nitrate reductase
Synechocystis sp., Thermosynechococcus sp.
-
-
nitrate reductase
Thermosynechococcus sp. BP-1
-
-
-
nitrate reductase
-
-
reductase, nitrate (ferredoxin)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
60382-69-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
previously classified as Nostoc muscorum 7119, filamentous nitrogen fixer; strain 7119
-
-
Manually annotated by BRENDA team
strain 7119; strains 7120 and M131
-
-
Manually annotated by BRENDA team
strain PCC 7120
-
-
Manually annotated by BRENDA team
Anabaena sp. 7119
strain 7119
-
-
Manually annotated by BRENDA team
strain ATCC 29413
-
-
Manually annotated by BRENDA team
strains 7101 and 7601
-
-
Manually annotated by BRENDA team
heterocystous nitrogen-fixing cyanobacterial strains
-
-
Manually annotated by BRENDA team
strain N1, phototrophic, purple sulfur bacterium
-
-
Manually annotated by BRENDA team
Ectothiorhodospira shaposhnikovii N1
strain N1, phototrophic, purple sulfur bacterium
-
-
Manually annotated by BRENDA team
strain 1829
-
-
Manually annotated by BRENDA team
Fischerella muscicola 1829
strain 1829
-
-
Manually annotated by BRENDA team
extreme halophilic archaeon
-
-
Manually annotated by BRENDA team
strain 7119
-
-
Manually annotated by BRENDA team
Nostoc muscorum 7119
strain 7119
-
-
Manually annotated by BRENDA team
strain PCC 6719, filamentous nitrogen fixer
-
-
Manually annotated by BRENDA team
strains 29105 and 29150
-
-
Manually annotated by BRENDA team
strain CU 1462/7
-
-
Manually annotated by BRENDA team
Phormidium uncinatum CU 1462/7
strain CU 1462/7
-
-
Manually annotated by BRENDA team
formerly known as Anacystis nidulans
-
-
Manually annotated by BRENDA team
strain L 1402-1; unicellular non-nitrogen fixer
-
-
Manually annotated by BRENDA team
Synechococcus elongatus PCC 7942 L 1402-1
strain L 1402-1
-
-
Manually annotated by BRENDA team
strain PCC 7942
-
-
Manually annotated by BRENDA team
strain PCC 7942
SwissProt
Manually annotated by BRENDA team
strain WH 8102
-
-
Manually annotated by BRENDA team
Synechococcus sp. WH
strain WH 8102
-
-
Manually annotated by BRENDA team
strain 6803, unicellular cyanobacterium
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
Synechocystis sp. 6803
strain 6803, unicellular cyanobacterium
-
-
Manually annotated by BRENDA team
Thermosynechococcus sp.
strain BP-1
-
-
Manually annotated by BRENDA team
Thermosynechococcus sp. BP-1
strain BP-1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
P39458, -
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
100 nM dithionite reduced ferredoxin with 94% of the activity with reduced methyl viologen
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
enzyme can not accept electrons directly from NAD(P)H, it is dependent on reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
ratio of methyl viologen- to ferredoxin-dependent nitrate reduction is about 27
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
depends on reduced ferredoxin for its activity, multimodal kinetic model: a single catalytic site functions in multiple kinetic modes
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
ferredoxin as electron donor at neutral pH and pH 8, but not at pH 9
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
coupled ferredoxin-NADPH reductase activity with NADP+-reductase system
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
coupled ferredoxin-NADPH reductase activity with NADP+-reductase system
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
spinach ferredoxin or Anabaena ferredoxin
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Ectothiorhodospira shaposhnikovii N1
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Nostoc muscorum 7119
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Synechococcus sp. WH
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Anabaena sp. 7119
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Anabaena sp. 7119, Synechocystis sp. 6803
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Thermosynechococcus sp. BP-1
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Fischerella muscicola 1829
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
Phormidium uncinatum CU 1462/7
-
coupled ferredoxin-NADPH reductase activity with NADP+-reductase system
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
two-electron nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
nitrate assimilation, ferredoxin-dependent photosynthetic reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
nitrate fermentation, ferredoxin is utilized as direct electron donor in nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Nostoc muscorum 7119
-
nitrate assimilation, ferredoxin-dependent photosynthetic reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Anabaena sp. 7119
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Anabaena sp. 7119
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced flavodoxin
nitrite + oxidized flavodoxin + H2O
show the reaction diagram
-
flavodoxin can physiologically substitute for ferredoxin under conditions of iron starvation
-
-
-
nitrate + reduced flavodoxin
nitrite + H2O + oxidized flavodoxin
show the reaction diagram
Synechococcus sp., Anabaena sp., Synechocystis sp., Nostoc punctiforme, Gloeobacter violaceus, Synechococcus elongatus, Trichodesmium erythraeum, Thermosynechococcus sp., Synechococcus sp. WH, Thermosynechococcus sp. BP-1
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
nitrite formation 10times higher at pH 9 than at pH 8
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
reduced methyl viologen is the best electron donor in vitro
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme also has methyl viologen-linked activity
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme also has methyl viologen-linked activity
-
-
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
-
enzyme also has methyl viologen-linked activity
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Ectothiorhodospira shaposhnikovii N1
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Anabaena sp. 7119
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Anabaena sp. 7119
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Synechocystis sp. 6803, Fischerella muscicola 1829
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
enzyme uses also reduced methyl viologen as reductant
-
?
nitrate + reduced methyl viologen
nitrite + H2O + oxidized methyl viologen
show the reaction diagram
Synechococcus sp., Anabaena sp., Synechocystis sp., Nostoc punctiforme, Gloeobacter violaceus, Synechococcus elongatus, Trichodesmium erythraeum, Thermosynechococcus sp., Synechococcus sp. WH, Thermosynechococcus sp. BP-1
-
-
-
-
?
nitrate + reduced methylviologen
nitrite + H2O + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methylviologen
selenite + H2O + oxidized methylviologen
show the reaction diagram
-
1% of kcat with nitrate
-
-
?
chlorate + reduced methylviologen
chlorite + H2O + oxidized methylviologen
show the reaction diagram
-
6% of kcat with nitrate
-
-
?
additional information
?
-
-
not as electron donors: NADH, NADPH, FADH2, FMNH2, rubredoxin
-
-
-
additional information
?
-
-
not as electron donors: NADH, NADPH, dithionite, 8% of maximum activity with 1mM FADH2 and less than 7% of maximum activity with 1 mM reduced 2,6-dichlorophenolindophenol or phenazine methosulfate
-
-
-
additional information
?
-
Ectothiorhodospira shaposhnikovii, Ectothiorhodospira shaposhnikovii N1
-
not as electron donors: NADH, NADPH, FADH2, FMNH2, reduced animal cytochrome c, sodium dithionite, methylene blue, phenazine methosulfate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
nitrate + reduced ferredoxin
nitrite + H2O + oxidized ferredoxin
show the reaction diagram
P39458, -
-
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
assimilatory nitrate reduction
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
two-electron nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
nitrate assimilation, ferredoxin-dependent photosynthetic reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
reduced ferredoxin as physiological electron donor
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
nitrate fermentation, ferredoxin is utilized as direct electron donor in nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Nostoc muscorum 7119
-
nitrate assimilation, ferredoxin-dependent photosynthetic reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Anabaena sp. 7119
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Anabaena sp. 7119
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
assimilatory nitrate reduction
-
-
?
nitrate + reduced ferredoxin
nitrite + oxidized ferredoxin
show the reaction diagram
Synechococcus elongatus PCC 7942 L 1402-1
-
first step in assimilatory reduction of nitrate
-
?
nitrate + reduced flavodoxin
nitrite + oxidized flavodoxin + H2O
show the reaction diagram
-
flavodoxin can physiologically substitute for ferredoxin under conditions of iron starvation
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Heme c
-
enzyme contains 1.5 heme molecules of the c-type
iron-sulfur centre
-
contains 4 iron and 4 acid-labile sulfur atoms per enzyme molecule, presence of iron-sulfur cluster
iron-sulfur centre
-
enzyme contains Fe-S clusters
molybdenum cofactor
-
-
molybdopterin
P39458, -
bis-molybdopterin guanine dinucleotide
additional information
-
no presence of flavin, heme or cytochrome
-
additional information
-
no FAD or cytochromes are observed
-
additional information
-
narB gene with domains that might be involved in binding of the molybdenum cofactor and of an iron-sulfur cluster, but no flavin nucleotide- or heme-binding domains
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
stimulates activity about 30%
Fe2+
-
stimulates activity about 50%
Iron
-
contains 4 iron and 4 acid-labile sulfur atoms per enzyme molecule; molybdenum iron-sulfur protein
Iron
-
molybdenum iron-sulfur protein
Iron
-
enzyme contains one iron sulfur cluster
Iron
-
nitrate reductase contains 1 [4Fe-4S] cluster
Iron
P39458, -
enzyme contains 1 [3Fe-4S] cluster
iron-sulfur centre
-
contains 4 iron and 4 acid-labile sulfur atoms per enzyme molecule, presence of iron-sulfur cluster
iron-sulfur centre
-
molybdo-iron-sulfur protein
iron-sulfur centre
-
enzyme contains Fe-S clusters
Mg2+
-
stimulates activity about 30%
Mn2+
-
stimulates activity about 50%, stimulates reaction rate and level of nitrite formation
Molybdenum
-
enzyme contains one molybdenum atom; molybdoprotein
Molybdenum
-
essential role in catalytic activity; molybdoprotein
Molybdenum
-
Mo center
Molybdenum
-
enzyme contains 0.95 atom of molybdenum per enzyme molecule; molybdenum iron-sulfur protein
Molybdenum
-
molybdenum iron-sulfur protein
Molybdenum
-
enzyme probably contains a bis-molybdopterin guanine dinucleotide
Molybdenum
-
-
Molybdenum
P39458, -
1 atom of Mo and 2 molecules of ribonucleotide-conjugated molybdopterin per molecule of protein
NaCl
-
activity depends on salt concentration
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ammonia
-
after initial slight stimulation rapid and complete inhibition, promotes conversion of ferredoxin-nitrate reductase into its reduced inactive form, metabolic interconversion
azide
-
competitive inhibitor
azide
-
74% inhibition
azide
-
potent inhibitor, 79% loss of activity
azide
-
competitive inhibition
cyanide
-
powerful inhibitor
cyanide
-
competitive inhibitor
cyanide
-
10 mM, 87% inhibition
cyanide
-
almost complete inhibition
cyanide
-
mixed inhibition, 50% inhibition at 0.01 mM
Dithionite
-
inactivation can be suppressed by cyanide and azide and specifically prevented by superoxide dismutase
Dithionite
-
converts native enzyme in modified form without ferredoxin-linked activity but retained methyl viologen-linked activity
EDTA
-
photoactivated EDTA, irreversible inactivation
EDTA
-
partial inhibition, 43% loss of activity
FAD
-
photoactivated FAD, irreversible inactivation
KCl
-
inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
light
-
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
-
N-acetylsuccinimide
-
115fold excess, loss of more than 80% and 5-10% loss of ferredoxin-dependent and methylviologen dependent activity after 1 h, respectively
NaCl
-
more than 80% inhibition above 200 mM, inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
oxygen
-
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
-
powerful inhibitor
Phenylglyoxal
-
76fold excess, approx. 60% and 20% loss of ferredoxin dependent and methylviologen dependent activity after 2 h, respectively
MgSO4
-
inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
additional information
-
nitrate plays an active role in enzyme synthesis, ammonia acts as antagonist
-
additional information
-
enzyme synthesis is repressed in presence of ammonia as a result of its metabolism, nitrate is not required as an obligate inducer
-
additional information
-
not inhibited by 0.1 mM p-chloromercuribenzoate, enzyme formation is induced by nitrate and inhibited by 0.5 mM tungstate, but recovered by 0.1 mM molybdate
-
additional information
-
not inhibited by potassium chlorate, dithiothreitol, p-hydroxymercuribenzoate, sulfite
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
nitrate plays an active role in enzyme synthesis, ammonia acts as antagonist
-
additional information
-
enzyme synthesis is induced by nitrate
-
additional information
-
enzyme synthesis is induced by nitrate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05
-
nitrate
-
25C, pH 8.0, electron donor methylviologen
-
0.1
-
nitrate
-
-
-
0.7
2.1
nitrate
-
-
-
0.95
-
nitrate
-
-
-
1.5
-
nitrate
-
reduced methyl viologen as electron donor, recombinant enzyme expressed in Escherichia coli
-
0.013
-
reduced ferredoxin
-
-
0.038
-
reduced ferredoxin
-
-
0.066
-
reduced methyl viologen
-
-
2.5
-
reduced methyl viologen
-
-
0.05
-
Ferredoxin
-
spinach ferredoxin
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
80
-
nitrate
-
25C, pH 8.0, electron donor methylviologen
-
1090
-
nitrate
-
dithionite-reduced methyl viologen as electron donor
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13
-
azide
-
25C, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.2
-
-
in situ assay, cells grown on media containing nitrate
305
-
-
ferredoxin-linked activity
1020
-
-
methyl viologen-linked activity
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
anaerobic assay, methyl viologen- and ferredoxin-linked activity
9
-
-
reduced methyl viologen as electron donor
9.5
10.5
-
reduced methyl viologen as electron donor
10.2
-
-
aerobic assay, methyl viologen-linked activity
10.5
-
-
dithionite-reduced methyl viologen as electron donor
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.3
9.2
-
at pH 7.3 and 9.2: 50% of activity maximum, aerobic assay, methyl viologen-linked and ferredoxin-linked activity
8.3
9.8
-
at pH 8.3 and 9.8: about 50% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
37
-
-
reduced methyl viologen as electron donor
60
-
-
for NaCl concentrations of 1.3 and 0.9 M
80
-
-
for NaCl concentrations of 3.1 and 2.2 M
additional information
-
-
assay at room temperature
additional information
-
-
strong dependence of activity on the temperature and NaCl concentrations
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme functions in the soluble state in the cytoplasm
Manually annotated by BRENDA team
-
recombinant enzyme activity is found exclusively in the soluble fraction
-
Manually annotated by BRENDA team
Synechococcus sp. WH, Thermosynechococcus sp. BP-1
-
-
-
Manually annotated by BRENDA team
-
tightly bound to chlorophyll-containing membrane fractions
Manually annotated by BRENDA team
additional information
-
activity remains associated with photosynthetic subcellular particles
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80000
-
-
gel filtration
85000
-
-
sedimentation equilibrium method
90000
-
-
ultracentrifugation
132000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 76000, enzyme expressed in Escherichia coli, SDS-PAGE
?
-
x * 76000, deduced from nucleotide sequence
?
-
x * 78000, SDS-PAGE
dimer
-
2 * 85000
dimer
-
1 * 105000 + 1 * 50000, SDS-PAGE
monomer
-
1 * 83000, SDS-PAGE
monomer
-
1 * 90000, SDS-PAGE
monomer
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
5 min, crude extract, stable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
low ionic strength, 70 h, 0.002 mg protein/ml, 10 mM phosphate buffer or 50 mM Tris-HCl buffer, pH 7.5, unstable
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
440443
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 50 mM phosphate buffer, pH 7, 20% glycerol, 2 weeks, no loss of activity
-
-20C, in 50 mM Tris-HCl buffer, pH 7.5, 0.5 M NaCl, 1 mM EDTA, 1 month, no loss of activity
-
-20C, 20% glycerol, several months, no loss of activity
P39458, -
4C, several weeks, no loss of activity
P39458, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
185fold partial purification
-
purified from a few cyanobacterial strains
-
177fold purification
-
19000fold purification
-
recombinant enzyme
P39458, -
recombinant His-tagged nitrate reductase, Ni2+-affinity column
-
recombinant nitrate reductase
-
partial purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
strain 7120: gene encoding nitrate reductase is cloned and its complete amino acid sequence deduced
-
expression in Escherichia coli
P39458, -
expression of His-tagged nitrate reductase in Escherichia coli
-
expression of native and His-tagged nitrate reductase in Escherichia coli
-
narB structural gene for nitrate reductase is cloned and expressed in Escherichia coli as a 76 kDa polypeptide with 729 amino acids
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C12A
P39458, -
no actiivty, no iron-sulfur cluster
C16S
P39458, -
1.9% of wild type activity with ferredoxin, no iron-sulfur cluster
C56A
P39458, -
no activity, no iron-sulfur cluster
C56S
P39458, -
70% of wild type activity with ferredoxin, contains an iron-sulfur cluster
C9A
P39458, -
no activity, no iron-sulfur cluster
C9H
P39458, -
no narB expression