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Literature summary extracted from

  • Vazquez-Torres, A.; Baeumler, A.J.
    Nitrate, nitrite and nitric oxide reductases from the last universal common ancestor to modern bacterial pathogens (2016), Curr. Opin. Microbiol., 29, 1-8 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.5.1 gene narG Mycobacterium tuberculosis
1.7.5.1 gene narG in the narGHI gene cluster Escherichia coli
1.7.5.1 gene narG in the narGHI gene cluster Salmonella enterica subsp. enterica serovar Typhimurium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.5.1 cytosol
-
Escherichia coli 5829
-
1.7.5.1 cytosol
-
Mycobacterium tuberculosis 5829
-
1.7.5.1 cytosol
-
Salmonella enterica subsp. enterica serovar Typhimurium 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.5.1 Fe2+ the enzyme binds one [4Fe-4S] cluster per subunit Escherichia coli
1.7.5.1 Fe2+ the enzyme binds one [4Fe-4S] cluster per subunit Mycobacterium tuberculosis
1.7.5.1 Fe2+ the enzyme binds one [4Fe-4S] cluster per subunit Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 Molybdenum the enzyme contains one molybdenum-bis(molybdopterin guanine dinucleotide) cofactor per subunit Escherichia coli
1.7.5.1 Molybdenum the enzyme contains one molybdenum-bis(molybdopterin guanine dinucleotide) cofactor per subunit Mycobacterium tuberculosis
1.7.5.1 Molybdenum the enzyme contains one molybdenum-bis(molybdopterin guanine dinucleotide) cofactor per subunit Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.5.1 nitrite + ubiquinone + H2O Escherichia coli
-
nitrate + ubiquinol
-
?
1.7.5.1 nitrite + ubiquinone + H2O Mycobacterium tuberculosis
-
nitrate + ubiquinol
-
?
1.7.5.1 nitrite + ubiquinone + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
nitrate + ubiquinol
-
?
1.7.5.1 nitrite + ubiquinone + H2O Mycobacterium tuberculosis H37Rv
-
nitrate + ubiquinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.7.5.1 Escherichia coli P09152 nitrate reductase 1 alpha subunit
-
1.7.5.1 Mycobacterium tuberculosis P9WJQ3 nitrate reductase alpha subunit
-
1.7.5.1 Mycobacterium tuberculosis H37Rv P9WJQ3 nitrate reductase alpha subunit
-
1.7.5.1 Salmonella enterica subsp. enterica serovar Typhimurium Q8ZP37 nitrate reductase 1 alpha subunit
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.5.1 nitrite + ubiquinone + H2O
-
Escherichia coli nitrate + ubiquinol
-
?
1.7.5.1 nitrite + ubiquinone + H2O
-
Mycobacterium tuberculosis nitrate + ubiquinol
-
?
1.7.5.1 nitrite + ubiquinone + H2O
-
Salmonella enterica subsp. enterica serovar Typhimurium nitrate + ubiquinol
-
?
1.7.5.1 nitrite + ubiquinone + H2O
-
Mycobacterium tuberculosis H37Rv nitrate + ubiquinol
-
?

Synonyms

EC Number Synonyms Comment Organism
1.7.5.1 NarG
-
Escherichia coli
1.7.5.1 NarG
-
Mycobacterium tuberculosis
1.7.5.1 NarG
-
Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 nitrate reducatse A
-
Escherichia coli
1.7.5.1 nitrate reducatse A
-
Mycobacterium tuberculosis
1.7.5.1 nitrate reducatse A
-
Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.5.1 flavin a flavoprotein Escherichia coli
1.7.5.1 flavin a flavoprotein Mycobacterium tuberculosis
1.7.5.1 flavin a flavoprotein Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 molybdenum bis-molybdopterin guanine dinucleotide the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit Escherichia coli
1.7.5.1 molybdenum bis-molybdopterin guanine dinucleotide the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit Mycobacterium tuberculosis
1.7.5.1 molybdenum bis-molybdopterin guanine dinucleotide the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 NAD+
-
Escherichia coli
1.7.5.1 NAD+
-
Mycobacterium tuberculosis
1.7.5.1 NAD+
-
Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 NADH
-
Escherichia coli
1.7.5.1 NADH
-
Mycobacterium tuberculosis
1.7.5.1 NADH
-
Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 ubiquinone
-
Escherichia coli
1.7.5.1 ubiquinone
-
Mycobacterium tuberculosis
1.7.5.1 ubiquinone
-
Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 [4Fe-4S] cluster the enzyme binds one [4Fe-4S] cluster per subunit Escherichia coli
1.7.5.1 [4Fe-4S] cluster the enzyme binds one [4Fe-4S] cluster per subunit Mycobacterium tuberculosis
1.7.5.1 [4Fe-4S] cluster the enzyme binds one [4Fe-4S] cluster per subunit Salmonella enterica subsp. enterica serovar Typhimurium

Expression

EC Number Organism Comment Expression
1.7.5.1 Escherichia coli nitrate reductase A is synthesized optimally at NO3- concentrations of 10 mM or above up
1.7.5.1 Salmonella enterica subsp. enterica serovar Typhimurium nitrate reductase A is synthesized optimally at NO3- concentrations of 10 mM or above up

General Information

EC Number General Information Comment Organism
1.7.5.1 metabolism nitrate enters the periplasm through porins where it is reduced to nitrite by the periplasmic nitrate reductase (Nap) or it is further transported into the bacterial cytosol by NarK and serves as an electron acceptor for nitrate reductase A (NarG). Periplasmic nitrite is further converted to NH3 by the periplasmic nitrite reductase (Nrf). Electrons required for these reactions can be transferred to the quinone (Q) pool by NADH:ubiquinone oxidoreductase (Nuo) in a reaction coupled to energy-conserving proton translocation Escherichia coli
1.7.5.1 metabolism nitrate enters the periplasm through porins where it is reduced to nitrite by the periplasmic nitrate reductase (Nap) or it is further transported into the bacterial cytosol by NarK and serves as an electron acceptor for nitrate reductase A (NarG). Periplasmic nitrite is further converted to NH3 by the periplasmic nitrite reductase (Nrf). Electrons required for these reactions can be transferred to the quinone (Q) pool by NADH:ubiquinone oxidoreductase (Nuo) in a reaction coupled to energy-conserving proton translocation Mycobacterium tuberculosis
1.7.5.1 metabolism nitrate enters the periplasm through porins where it is reduced to nitrite by the periplasmic nitrate reductase (Nap) or it is further transported into the bacterial cytosol by NarK and serves as an electron acceptor for nitrate reductase A (NarG). Periplasmic nitrite is further converted to NH3 by the periplasmic nitrite reductase (Nrf). Electrons required for these reactions can be transferred to the quinone (Q) pool by NADH:ubiquinone oxidoreductase (Nuo) in a reaction coupled to energy-conserving proton translocation Salmonella enterica subsp. enterica serovar Typhimurium
1.7.5.1 physiological function the NO2- that arises from human host-derived NO3- through the enzymatic activity of Mycobacterium tuberculosis enzyme NarG inhibits bacterial growth, enhances ATP synthesis, and regulates the expression of 120 genes associated with adaptation to acid, hypoxia, oxidative and nitrosative stress, and iron deprivation. Enzyme NarG can promote growth of this intracellular pathogen in NO-producing human macrophages. Importance of NO3-/NO2- reduction in the pathogenesis. Bis-molybdopterin guanine dinucleotide, the cofactor of nitrate reductase, is required for the persistence of intracellular pathogen Mycobacterium tuberculosis in guinea pigs. The enzymatic activity of Mycobacterium tuberculosis NarG inhibits bacterial growth Mycobacterium tuberculosis