1.9.6.1: nitrate reductase (cytochrome)
This is an abbreviated version!
For detailed information about nitrate reductase (cytochrome), go to the full flat file.
Word Map on EC 1.9.6.1
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1.9.6.1
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nitrite
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denitrification
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denitrify
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molybdenum
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paracoccus
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dissimilatory
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denitrificans
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n2o
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pantotrophus
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napf
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nitrate-reducing
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desulfuricans
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molybdoenzymes
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thiosphaera
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cyma
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fixk2
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menaquinol
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di-haem
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bismolybdopterin
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wolinella
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high-g
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narghi
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norcbqd
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nitrate-dependent
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mo-containing
- 1.9.6.1
- nitrite
-
denitrification
-
denitrify
- molybdenum
- paracoccus
-
dissimilatory
- denitrificans
- n2o
- pantotrophus
- napf
-
nitrate-reducing
- desulfuricans
-
molybdoenzymes
-
thiosphaera
-
cyma
- fixk2
- menaquinol
-
di-haem
-
bismolybdopterin
-
wolinella
-
high-g
- narghi
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norcbqd
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nitrate-dependent
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mo-containing
Reaction
2 ferrocytochrome + 2 H+ + = 2 ferricytochrome + +
Synonyms
benzyl viologen-nitrate reductase, EC 1.7.99.4, mmol_1648, More, NAP, NAP enzyme, Nap-alpha, NAP-beta, NapA, napA-beta, NapAB, NapABC, NapDAGHB, NapEDABC, nitrate reductase, periplasmic, periplasmic nitrate reductase, periplasmic nitrate reductases, reductase, nitrate (cytochrome), respiratory nitrate reductase, single subunit Nap-type periplasmic nitrate reductase
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Subunits
Subunits on EC 1.9.6.1 - nitrate reductase (cytochrome)
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heterodimer
additional information
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x * 90000 + x * 16000, two-subunit complex, NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster. NapB is an 16000 Da electron-transfer subunit, which in other bacteria binds two c-type haems
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1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively
heterodimer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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1 * 17000 + 1 * 87000, SDS-PAGE
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heterodimer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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1 * 93309 + 1 * 18924, calculated from sequence
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heterodimer
P33937; P0ABL3
1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE
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
additional information
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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
additional information
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
additional information
-
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
-
additional information
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
additional information
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
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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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
-
additional information
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
additional information
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
additional information
PELDOR analysis of recombinant MTSL-labelled MalE-NapASP fusion mutant S4C/S24C alone or in complex with NapD, comparison of bound, NMR-derived NapASP helix from PDB ID 2PQ4 versus free generated helix, positions of the spin labels in the two conformations of the signal peptide, overview
additional information
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PELDOR analysis of recombinant MTSL-labelled MalE-NapASP fusion mutant S4C/S24C alone or in complex with NapD, comparison of bound, NMR-derived NapASP helix from PDB ID 2PQ4 versus free generated helix, positions of the spin labels in the two conformations of the signal peptide, overview
additional information
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
additional information
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the nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase, encodes seven proteins. The catalytic complex in the periplasm, NapANapB receives electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, NapD, is also essential for Nap activity. None of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-heme, iron-sulfur proteins, are essential for Nap activity
additional information
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
additional information
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
additional information
-
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
-
additional information
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
additional information
-
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
-
additional information
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
additional information
-
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
additional information
-
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