Literature summary for 1.9.6.1 extracted from

Gonzalez, P.; Rivas, M.; Mota, C.; Brondino, C.; Moura, I.; Moura, J.
Periplasmic nitrate reductases and formate dehydrogenases biological control of the chemical properties of Mo and W for fine tuning of reactivity, substrate specificity and metabolic role (2013), Coord. Chem. Rev., 257, 315-331 .

No PubMed abstract available

Cloned(Commentary)

Cloned (Comment)	Organism
gene nap and nap gene cluster, genetic organization and sequence comparisons	Bradyrhizobium japonicum
gene nap and nap gene cluster, genetic organization and sequence comparisons	Wolinella succinogenes
gene nap and nap gene cluster, genetic organization and sequence comparisons	Shewanella oneidensis
gene nap and nap gene cluster, genetic organization and sequence comparisons	Desulfovibrio desulfuricans
gene nap and nap gene cluster, genetic organization and sequence comparisons	Paracoccus pantotrophus
gene nap and nap gene cluster, genetic organization and sequence comparisons	Pseudomonas sp.
gene nap and nap gene cluster, genetic organization and sequence comparisons	Cupriavidus necator
gene nap and nap gene cluster, genetic organization and sequence comparisons	Cereibacter sphaeroides
gene nap and nap gene cluster, genetic organization and sequence comparisons	Shewanella gelidimarina
gene nap and nap gene cluster, genetic organization and sequence comparisons	Desulfitobacterium hafniense
gene nap and nap gene cluster, genetic organization and sequence comparisons	Anaeromyxobacter dehalogenans
gene nap and nap gene cluster, genetic organization and sequence comparisons	Campylobacter jejuni subsp. jejuni
gene nap and nap gene cluster, genetic organization and sequence comparisons	Paracoccus denitrificans
gene nap and nap gene cluster, genetic organization and sequence comparisons	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Bradyrhizobium japonicum	-	-
periplasm	-	Wolinella succinogenes	-	-
periplasm	-	Shewanella oneidensis	-	-
periplasm	-	Desulfovibrio desulfuricans	-	-
periplasm	-	Paracoccus pantotrophus	-	-
periplasm	-	Pseudomonas sp.	-	-
periplasm	-	Cupriavidus necator	-	-
periplasm	-	Cereibacter sphaeroides	-	-
periplasm	-	Shewanella gelidimarina	-	-
periplasm	-	Desulfitobacterium hafniense	-	-
periplasm	-	Anaeromyxobacter dehalogenans	-	-
periplasm	-	Campylobacter jejuni subsp. jejuni	-	-
periplasm	-	Paracoccus denitrificans	-	-
periplasm	-	Escherichia coli	-	-

Metals/Ions

Metals/Ions	Comment	Organism
Fe2+	in the heme/cytochrome cofactor	Bradyrhizobium japonicum
Fe2+	in the heme/cytochrome cofactor	Wolinella succinogenes
Fe2+	in the heme/cytochrome cofactor	Shewanella oneidensis
Fe2+	in the heme/cytochrome cofactor	Desulfovibrio desulfuricans
Fe2+	in the heme/cytochrome cofactor	Paracoccus pantotrophus
Fe2+	in the heme/cytochrome cofactor	Pseudomonas sp.
Fe2+	in the heme/cytochrome cofactor	Cupriavidus necator
Fe2+	in the heme/cytochrome cofactor	Cereibacter sphaeroides
Fe2+	in the heme/cytochrome cofactor	Shewanella gelidimarina
Fe2+	in the heme/cytochrome cofactor	Desulfitobacterium hafniense
Fe2+	in the heme/cytochrome cofactor	Anaeromyxobacter dehalogenans
Fe2+	in the heme/cytochrome cofactor	Campylobacter jejuni subsp. jejuni
Fe2+	in the heme/cytochrome cofactor	Paracoccus denitrificans
Fe2+	in the heme/cytochrome cofactor	Escherichia coli
Mo(VI)	-	Bradyrhizobium japonicum
Mo(VI)	-	Wolinella succinogenes
Mo(VI)	-	Shewanella oneidensis
Mo(VI)	-	Desulfitobacterium hafniense
Mo(VI)	-	Anaeromyxobacter dehalogenans
Mo(VI)	-	Campylobacter jejuni subsp. jejuni
Mo(VI)	-	Paracoccus denitrificans
Mo(VI)	coordinates a cysteine and a sulfido residue	Desulfovibrio desulfuricans
Mo(VI)	coordinates a cysteine and a sulfido residue	Paracoccus pantotrophus
Mo(VI)	coordinates a cysteine and a sulfido residue	Pseudomonas sp.
Mo(VI)	coordinates a cysteine and a sulfido residue	Cupriavidus necator
Mo(VI)	coordinates a cysteine and a sulfido residue	Cereibacter sphaeroides
Mo(VI)	coordinates a cysteine and a sulfido residue	Shewanella gelidimarina
Mo(VI)	coordinates a cysteine and a sulfido residue	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2 ferrocytochrome + 2 H+ + nitrate	Bradyrhizobium japonicum	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Wolinella succinogenes	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Shewanella oneidensis	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Desulfovibrio desulfuricans	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Paracoccus pantotrophus	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Pseudomonas sp.	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Cupriavidus necator	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Cereibacter sphaeroides	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Shewanella gelidimarina	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Desulfitobacterium hafniense	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Anaeromyxobacter dehalogenans	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Campylobacter jejuni subsp. jejuni	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Paracoccus denitrificans	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Escherichia coli	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Campylobacter jejuni subsp. jejuni ATCC 700819	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Pseudomonas sp. G-179	-	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	Paracoccus pantotrophus GB17	-	2 ferricytochrome + nitrite	-	?

Organism

Organism	UniProt	Comment	Textmining
Anaeromyxobacter dehalogenans	Q2IPE7	-	-
Bradyrhizobium japonicum	-	-	-
Campylobacter jejuni subsp. jejuni	Q9PPD9	-	-
Campylobacter jejuni subsp. jejuni ATCC 700819	Q9PPD9	-	-
Cereibacter sphaeroides	Q53176	-	-
Cupriavidus necator	P39185	-	-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	P39185	-	-
Desulfitobacterium hafniense	A0A098B5Y5	-	-
Desulfovibrio desulfuricans	P81186	-	-
Escherichia coli	P33937	-	-
Paracoccus denitrificans	A1BB88	-	-
Paracoccus pantotrophus	Q56350	-	-
Paracoccus pantotrophus GB17	Q56350	-	-
Pseudomonas sp.	Q9RC05	-	-
Pseudomonas sp. G-179	Q9RC05	-	-
Shewanella gelidimarina	E2F391	-	-
Shewanella oneidensis	-	-	-
Wolinella succinogenes	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Bradyrhizobium japonicum	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Wolinella succinogenes	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Shewanella oneidensis	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Desulfitobacterium hafniense	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Anaeromyxobacter dehalogenans	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Campylobacter jejuni subsp. jejuni	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Paracoccus denitrificans	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Desulfovibrio desulfuricans	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Paracoccus pantotrophus	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Pseudomonas sp.	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Cupriavidus necator	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Cereibacter sphaeroides	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Shewanella gelidimarina	a
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O	sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2 ferrocytochrome + 2 H+ + nitrate	-	Bradyrhizobium japonicum	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Wolinella succinogenes	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Shewanella oneidensis	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Desulfovibrio desulfuricans	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Paracoccus pantotrophus	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Pseudomonas sp.	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Cupriavidus necator	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Cereibacter sphaeroides	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Shewanella gelidimarina	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Desulfitobacterium hafniense	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Anaeromyxobacter dehalogenans	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Campylobacter jejuni subsp. jejuni	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Paracoccus denitrificans	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Escherichia coli	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Campylobacter jejuni subsp. jejuni ATCC 700819	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Pseudomonas sp. G-179	2 ferricytochrome + nitrite	-	?
2 ferrocytochrome + 2 H+ + nitrate	-	Paracoccus pantotrophus GB17	2 ferricytochrome + nitrite	-	?

Subunits

Subunits	Comment	Organism
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Bradyrhizobium japonicum
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Wolinella succinogenes
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Shewanella oneidensis
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Desulfovibrio desulfuricans
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Paracoccus pantotrophus
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Pseudomonas sp.
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Cupriavidus necator
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Cereibacter sphaeroides
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Shewanella gelidimarina
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Desulfitobacterium hafniense
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Anaeromyxobacter dehalogenans
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Campylobacter jejuni subsp. jejuni
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Paracoccus denitrificans
More	the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
NAP	-	Bradyrhizobium japonicum
NAP	-	Wolinella succinogenes
NAP	-	Shewanella oneidensis
NAP	-	Desulfovibrio desulfuricans
NAP	-	Paracoccus pantotrophus
NAP	-	Pseudomonas sp.
NAP	-	Cupriavidus necator
NAP	-	Cereibacter sphaeroides
NAP	-	Shewanella gelidimarina
NAP	-	Desulfitobacterium hafniense
NAP	-	Anaeromyxobacter dehalogenans
NAP	-	Campylobacter jejuni subsp. jejuni
NAP	-	Paracoccus denitrificans
NAP	-	Escherichia coli
NapA	-	Bradyrhizobium japonicum
NapA	-	Wolinella succinogenes
NapA	-	Shewanella oneidensis
NapA	-	Desulfovibrio desulfuricans
NapA	-	Paracoccus pantotrophus
NapA	-	Pseudomonas sp.
NapA	-	Cupriavidus necator
NapA	-	Cereibacter sphaeroides
NapA	-	Shewanella gelidimarina
NapA	-	Desulfitobacterium hafniense
NapA	-	Anaeromyxobacter dehalogenans
NapA	-	Campylobacter jejuni subsp. jejuni
NapA	-	Paracoccus denitrificans
NapA	-	Escherichia coli
napA-beta	-	Shewanella gelidimarina
periplasmic nitrate reductase	-	Bradyrhizobium japonicum
periplasmic nitrate reductase	-	Wolinella succinogenes
periplasmic nitrate reductase	-	Shewanella oneidensis
periplasmic nitrate reductase	-	Desulfovibrio desulfuricans
periplasmic nitrate reductase	-	Paracoccus pantotrophus
periplasmic nitrate reductase	-	Pseudomonas sp.
periplasmic nitrate reductase	-	Cupriavidus necator
periplasmic nitrate reductase	-	Cereibacter sphaeroides
periplasmic nitrate reductase	-	Shewanella gelidimarina
periplasmic nitrate reductase	-	Desulfitobacterium hafniense
periplasmic nitrate reductase	-	Anaeromyxobacter dehalogenans
periplasmic nitrate reductase	-	Campylobacter jejuni subsp. jejuni
periplasmic nitrate reductase	-	Paracoccus denitrificans
periplasmic nitrate reductase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism
cytochrome c	-	Bradyrhizobium japonicum
cytochrome c	-	Wolinella succinogenes
cytochrome c	-	Shewanella oneidensis
cytochrome c	-	Desulfitobacterium hafniense
cytochrome c	-	Anaeromyxobacter dehalogenans
cytochrome c	-	Campylobacter jejuni subsp. jejuni
cytochrome c	-	Paracoccus denitrificans
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Desulfovibrio desulfuricans
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Paracoccus pantotrophus
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Pseudomonas sp.
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Cupriavidus necator
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Cereibacter sphaeroides
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Shewanella gelidimarina
cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	Escherichia coli
molybdenum cofactor	-	Bradyrhizobium japonicum
molybdenum cofactor	-	Wolinella succinogenes
molybdenum cofactor	-	Shewanella oneidensis
molybdenum cofactor	-	Desulfitobacterium hafniense
molybdenum cofactor	-	Anaeromyxobacter dehalogenans
molybdenum cofactor	-	Campylobacter jejuni subsp. jejuni
molybdenum cofactor	-	Paracoccus denitrificans
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Desulfovibrio desulfuricans
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Paracoccus pantotrophus
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Pseudomonas sp.
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Cupriavidus necator
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Cereibacter sphaeroides
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Shewanella gelidimarina
molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	Escherichia coli
[4Fe-4S] cluster	-	Bradyrhizobium japonicum
[4Fe-4S] cluster	-	Wolinella succinogenes
[4Fe-4S] cluster	-	Shewanella oneidensis
[4Fe-4S] cluster	-	Desulfovibrio desulfuricans
[4Fe-4S] cluster	-	Paracoccus pantotrophus
[4Fe-4S] cluster	-	Pseudomonas sp.
[4Fe-4S] cluster	-	Cupriavidus necator
[4Fe-4S] cluster	-	Cereibacter sphaeroides
[4Fe-4S] cluster	-	Shewanella gelidimarina
[4Fe-4S] cluster	-	Desulfitobacterium hafniense
[4Fe-4S] cluster	-	Anaeromyxobacter dehalogenans
[4Fe-4S] cluster	-	Campylobacter jejuni subsp. jejuni
[4Fe-4S] cluster	-	Paracoccus denitrificans
[4Fe-4S] cluster	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Paracoccus pantotrophus
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Pseudomonas sp.
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Cupriavidus necator
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Cereibacter sphaeroides
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Shewanella gelidimarina
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Escherichia coli
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Bradyrhizobium japonicum
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Wolinella succinogenes
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Shewanella oneidensis
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Desulfitobacterium hafniense
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Anaeromyxobacter dehalogenans
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Campylobacter jejuni subsp. jejuni
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I	Paracoccus denitrificans
evolution	the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide	Desulfovibrio desulfuricans
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA, product of the napA gene, is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present	Desulfovibrio desulfuricans
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes	Paracoccus pantotrophus
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes	Pseudomonas sp.
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes	Cupriavidus necator
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes	Cereibacter sphaeroides
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes	Shewanella gelidimarina
additional information	the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present	Escherichia coli
physiological function	the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source	Paracoccus pantotrophus
physiological function	the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source	Cupriavidus necator
physiological function	the Nap enzyme from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source	Cereibacter sphaeroides
physiological function	the Nap enzyme from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source	Shewanella gelidimarina