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Information on EC 1.7.5.1 - nitrate reductase (quinone) and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WJQ3

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IUBMB Comments
A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WJQ3
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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nitrate
+
a quinol
=
nitrite
+
a quinone
+
H2O
+
=
+
+
Synonyms
membrane-bound nitrate reductase, narghi, nitrate reductase a, nitrate reductase z, quinol-nitrate oxidoreductase, quinol/nitrate oxidoreductase, quinol:nitrate oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrate reducatse A
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nitrite:quinone oxidoreductase
A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nitrite + ubiquinone + H2O
nitrate + ubiquinol
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nitrite + ubiquinone + H2O
nitrate + ubiquinol
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
a flavoprotein
molybdenum bis-molybdopterin guanine dinucleotide
the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit
[4Fe-4S] cluster
the enzyme binds one [4Fe-4S] cluster per subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the enzyme binds one [4Fe-4S] cluster per subunit
Molybdenum
the enzyme contains one molybdenum-bis(molybdopterin guanine dinucleotide) cofactor per subunit
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
nitrate reductase alpha subunit
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vazquez-Torres, A.; Baeumler, A.J.
Nitrate, nitrite and nitric oxide reductases from the last universal common ancestor to modern bacterial pathogens
Curr. Opin. Microbiol.
29
1-8
2016
Escherichia coli (P09152), Mycobacterium tuberculosis (P9WJQ3), Mycobacterium tuberculosis H37Rv (P9WJQ3), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZP37)
Manually annotated by BRENDA team