EC Number | Cloned (Comment) | Organism |
---|---|---|
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Bradyrhizobium japonicum |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Wolinella succinogenes |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Shewanella oneidensis |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Desulfovibrio desulfuricans |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Paracoccus pantotrophus |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Pseudomonas sp. |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Cupriavidus necator |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Cereibacter sphaeroides |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Shewanella gelidimarina |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Desulfitobacterium hafniense |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Anaeromyxobacter dehalogenans |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Campylobacter jejuni subsp. jejuni |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Paracoccus denitrificans |
1.9.6.1 | gene nap and nap gene cluster, genetic organization and sequence comparisons | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.9.6.1 | periplasm | - |
Bradyrhizobium japonicum | - |
- |
1.9.6.1 | periplasm | - |
Wolinella succinogenes | - |
- |
1.9.6.1 | periplasm | - |
Shewanella oneidensis | - |
- |
1.9.6.1 | periplasm | - |
Desulfovibrio desulfuricans | - |
- |
1.9.6.1 | periplasm | - |
Paracoccus pantotrophus | - |
- |
1.9.6.1 | periplasm | - |
Pseudomonas sp. | - |
- |
1.9.6.1 | periplasm | - |
Cupriavidus necator | - |
- |
1.9.6.1 | periplasm | - |
Cereibacter sphaeroides | - |
- |
1.9.6.1 | periplasm | - |
Shewanella gelidimarina | - |
- |
1.9.6.1 | periplasm | - |
Desulfitobacterium hafniense | - |
- |
1.9.6.1 | periplasm | - |
Anaeromyxobacter dehalogenans | - |
- |
1.9.6.1 | periplasm | - |
Campylobacter jejuni subsp. jejuni | - |
- |
1.9.6.1 | periplasm | - |
Paracoccus denitrificans | - |
- |
1.9.6.1 | periplasm | - |
Escherichia coli | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Bradyrhizobium japonicum | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Wolinella succinogenes | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Shewanella oneidensis | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Desulfovibrio desulfuricans | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Paracoccus pantotrophus | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Pseudomonas sp. | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Cupriavidus necator | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Cereibacter sphaeroides | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Shewanella gelidimarina | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Desulfitobacterium hafniense | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Anaeromyxobacter dehalogenans | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Campylobacter jejuni subsp. jejuni | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Paracoccus denitrificans | |
1.9.6.1 | Fe2+ | in the heme/cytochrome cofactor | Escherichia coli | |
1.9.6.1 | Mo(VI) | - |
Bradyrhizobium japonicum | |
1.9.6.1 | Mo(VI) | - |
Wolinella succinogenes | |
1.9.6.1 | Mo(VI) | - |
Shewanella oneidensis | |
1.9.6.1 | Mo(VI) | - |
Desulfitobacterium hafniense | |
1.9.6.1 | Mo(VI) | - |
Anaeromyxobacter dehalogenans | |
1.9.6.1 | Mo(VI) | - |
Campylobacter jejuni subsp. jejuni | |
1.9.6.1 | Mo(VI) | - |
Paracoccus denitrificans | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Desulfovibrio desulfuricans | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Paracoccus pantotrophus | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Pseudomonas sp. | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Cupriavidus necator | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Cereibacter sphaeroides | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Shewanella gelidimarina | |
1.9.6.1 | Mo(VI) | coordinates a cysteine and a sulfido residue | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Bradyrhizobium japonicum | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Wolinella succinogenes | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Shewanella oneidensis | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Desulfovibrio desulfuricans | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Paracoccus pantotrophus | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Pseudomonas sp. | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Cupriavidus necator | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Cereibacter sphaeroides | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Shewanella gelidimarina | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Desulfitobacterium hafniense | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Anaeromyxobacter dehalogenans | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Campylobacter jejuni subsp. jejuni | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Paracoccus denitrificans | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Escherichia coli | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Campylobacter jejuni subsp. jejuni ATCC 700819 | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Pseudomonas sp. G-179 | - |
2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | Paracoccus pantotrophus GB17 | - |
2 ferricytochrome + nitrite | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.9.6.1 | Anaeromyxobacter dehalogenans | Q2IPE7 | - |
- |
1.9.6.1 | Bradyrhizobium japonicum | - |
- |
- |
1.9.6.1 | Campylobacter jejuni subsp. jejuni | Q9PPD9 | - |
- |
1.9.6.1 | Campylobacter jejuni subsp. jejuni ATCC 700819 | Q9PPD9 | - |
- |
1.9.6.1 | Cereibacter sphaeroides | Q53176 | - |
- |
1.9.6.1 | Cupriavidus necator | P39185 | - |
- |
1.9.6.1 | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | P39185 | - |
- |
1.9.6.1 | Desulfitobacterium hafniense | A0A098B5Y5 | - |
- |
1.9.6.1 | Desulfovibrio desulfuricans | P81186 | - |
- |
1.9.6.1 | Escherichia coli | P33937 | - |
- |
1.9.6.1 | Paracoccus denitrificans | A1BB88 | - |
- |
1.9.6.1 | Paracoccus pantotrophus | Q56350 | - |
- |
1.9.6.1 | Paracoccus pantotrophus GB17 | Q56350 | - |
- |
1.9.6.1 | Pseudomonas sp. | Q9RC05 | - |
- |
1.9.6.1 | Pseudomonas sp. G-179 | Q9RC05 | - |
- |
1.9.6.1 | Shewanella gelidimarina | E2F391 | - |
- |
1.9.6.1 | Shewanella oneidensis | - |
- |
- |
1.9.6.1 | Wolinella succinogenes | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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. | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Bradyrhizobium japonicum | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Wolinella succinogenes | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Shewanella oneidensis | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Desulfovibrio desulfuricans | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Paracoccus pantotrophus | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Pseudomonas sp. | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Cupriavidus necator | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Cereibacter sphaeroides | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Shewanella gelidimarina | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Desulfitobacterium hafniense | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Anaeromyxobacter dehalogenans | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Campylobacter jejuni subsp. jejuni | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Paracoccus denitrificans | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Escherichia coli | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Campylobacter jejuni subsp. jejuni ATCC 700819 | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Pseudomonas sp. G-179 | 2 ferricytochrome + nitrite | - |
? | |
1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate | - |
Paracoccus pantotrophus GB17 | 2 ferricytochrome + nitrite | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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. |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.9.6.1 | NAP | - |
Bradyrhizobium japonicum |
1.9.6.1 | NAP | - |
Wolinella succinogenes |
1.9.6.1 | NAP | - |
Shewanella oneidensis |
1.9.6.1 | NAP | - |
Desulfovibrio desulfuricans |
1.9.6.1 | NAP | - |
Paracoccus pantotrophus |
1.9.6.1 | NAP | - |
Pseudomonas sp. |
1.9.6.1 | NAP | - |
Cupriavidus necator |
1.9.6.1 | NAP | - |
Cereibacter sphaeroides |
1.9.6.1 | NAP | - |
Shewanella gelidimarina |
1.9.6.1 | NAP | - |
Desulfitobacterium hafniense |
1.9.6.1 | NAP | - |
Anaeromyxobacter dehalogenans |
1.9.6.1 | NAP | - |
Campylobacter jejuni subsp. jejuni |
1.9.6.1 | NAP | - |
Paracoccus denitrificans |
1.9.6.1 | NAP | - |
Escherichia coli |
1.9.6.1 | NapA | - |
Bradyrhizobium japonicum |
1.9.6.1 | NapA | - |
Wolinella succinogenes |
1.9.6.1 | NapA | - |
Shewanella oneidensis |
1.9.6.1 | NapA | - |
Desulfovibrio desulfuricans |
1.9.6.1 | NapA | - |
Paracoccus pantotrophus |
1.9.6.1 | NapA | - |
Pseudomonas sp. |
1.9.6.1 | NapA | - |
Cupriavidus necator |
1.9.6.1 | NapA | - |
Cereibacter sphaeroides |
1.9.6.1 | NapA | - |
Shewanella gelidimarina |
1.9.6.1 | NapA | - |
Desulfitobacterium hafniense |
1.9.6.1 | NapA | - |
Anaeromyxobacter dehalogenans |
1.9.6.1 | NapA | - |
Campylobacter jejuni subsp. jejuni |
1.9.6.1 | NapA | - |
Paracoccus denitrificans |
1.9.6.1 | NapA | - |
Escherichia coli |
1.9.6.1 | napA-beta | - |
Shewanella gelidimarina |
1.9.6.1 | periplasmic nitrate reductase | - |
Bradyrhizobium japonicum |
1.9.6.1 | periplasmic nitrate reductase | - |
Wolinella succinogenes |
1.9.6.1 | periplasmic nitrate reductase | - |
Shewanella oneidensis |
1.9.6.1 | periplasmic nitrate reductase | - |
Desulfovibrio desulfuricans |
1.9.6.1 | periplasmic nitrate reductase | - |
Paracoccus pantotrophus |
1.9.6.1 | periplasmic nitrate reductase | - |
Pseudomonas sp. |
1.9.6.1 | periplasmic nitrate reductase | - |
Cupriavidus necator |
1.9.6.1 | periplasmic nitrate reductase | - |
Cereibacter sphaeroides |
1.9.6.1 | periplasmic nitrate reductase | - |
Shewanella gelidimarina |
1.9.6.1 | periplasmic nitrate reductase | - |
Desulfitobacterium hafniense |
1.9.6.1 | periplasmic nitrate reductase | - |
Anaeromyxobacter dehalogenans |
1.9.6.1 | periplasmic nitrate reductase | - |
Campylobacter jejuni subsp. jejuni |
1.9.6.1 | periplasmic nitrate reductase | - |
Paracoccus denitrificans |
1.9.6.1 | periplasmic nitrate reductase | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.9.6.1 | cytochrome c | - |
Bradyrhizobium japonicum | |
1.9.6.1 | cytochrome c | - |
Wolinella succinogenes | |
1.9.6.1 | cytochrome c | - |
Shewanella oneidensis | |
1.9.6.1 | cytochrome c | - |
Desulfitobacterium hafniense | |
1.9.6.1 | cytochrome c | - |
Anaeromyxobacter dehalogenans | |
1.9.6.1 | cytochrome c | - |
Campylobacter jejuni subsp. jejuni | |
1.9.6.1 | cytochrome c | - |
Paracoccus denitrificans | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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. | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | 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 | |
1.9.6.1 | molybdenum cofactor | - |
Bradyrhizobium japonicum | |
1.9.6.1 | molybdenum cofactor | - |
Wolinella succinogenes | |
1.9.6.1 | molybdenum cofactor | - |
Shewanella oneidensis | |
1.9.6.1 | molybdenum cofactor | - |
Desulfitobacterium hafniense | |
1.9.6.1 | molybdenum cofactor | - |
Anaeromyxobacter dehalogenans | |
1.9.6.1 | molybdenum cofactor | - |
Campylobacter jejuni subsp. jejuni | |
1.9.6.1 | molybdenum cofactor | - |
Paracoccus denitrificans | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Desulfovibrio desulfuricans | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Paracoccus pantotrophus | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Pseudomonas sp. | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Cupriavidus necator | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Cereibacter sphaeroides | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Shewanella gelidimarina | |
1.9.6.1 | molybdenum cofactor | synthesis of the Mo-pyranopterin cofactor, overview | Escherichia coli | |
1.9.6.1 | [4Fe-4S] cluster | - |
Bradyrhizobium japonicum | |
1.9.6.1 | [4Fe-4S] cluster | - |
Wolinella succinogenes | |
1.9.6.1 | [4Fe-4S] cluster | - |
Shewanella oneidensis | |
1.9.6.1 | [4Fe-4S] cluster | - |
Desulfovibrio desulfuricans | |
1.9.6.1 | [4Fe-4S] cluster | - |
Paracoccus pantotrophus | |
1.9.6.1 | [4Fe-4S] cluster | - |
Pseudomonas sp. | |
1.9.6.1 | [4Fe-4S] cluster | - |
Cupriavidus necator | |
1.9.6.1 | [4Fe-4S] cluster | - |
Cereibacter sphaeroides | |
1.9.6.1 | [4Fe-4S] cluster | - |
Shewanella gelidimarina | |
1.9.6.1 | [4Fe-4S] cluster | - |
Desulfitobacterium hafniense | |
1.9.6.1 | [4Fe-4S] cluster | - |
Anaeromyxobacter dehalogenans | |
1.9.6.1 | [4Fe-4S] cluster | - |
Campylobacter jejuni subsp. jejuni | |
1.9.6.1 | [4Fe-4S] cluster | - |
Paracoccus denitrificans | |
1.9.6.1 | [4Fe-4S] cluster | - |
Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.9.6.1 | 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 |
1.9.6.1 | 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. |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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. |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |
1.9.6.1 | 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 |