1.7.2.4: nitrous-oxide reductase
This is an abbreviated version!
For detailed information about nitrous-oxide reductase, go to the full flat file.
Word Map on EC 1.7.2.4
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1.7.2.4
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denitrification
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denitrify
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nitrite
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greenhouse
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denitrificans
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paracoccus
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stutzeri
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dinitrogen
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wastewater
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binuclear
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tetranuclear
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cycloclastes
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mixed-valence
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multicopper
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ammonia-oxidizing
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n-cycle
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nautica
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wolinella
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arable
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nitrospirae
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stratospheric
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agriculture
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t-rflp
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degradation
- 1.7.2.4
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denitrification
-
denitrify
- nitrite
-
greenhouse
- denitrificans
- paracoccus
- stutzeri
-
dinitrogen
-
wastewater
-
binuclear
-
tetranuclear
- cycloclastes
-
mixed-valence
-
multicopper
-
ammonia-oxidizing
-
n-cycle
- nautica
-
wolinella
-
arable
- nitrospirae
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stratospheric
- agriculture
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t-rflp
- degradation
Reaction
+ + = + 2 ferrocytochrome c + 2 H+
Synonyms
cNosZ, EC 1.7.99.6, HdN2OR, McoP, MhN2OR, multicopper oxidase, N(2)OR, N2O reductase, N2OR, nitrous oxide reductase, NosZ, PpN2OR, PsN2OR, Sden_2219, SdN2OR, Z-type N2OR
ECTree
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Subunits
Subunits on EC 1.7.2.4 - nitrous-oxide reductase
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dimer
homodimer
monomer
additional information
homodimer
Marinobacter nauticus
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2 * ?, each monomer is composed of two domains, a C-terminal cupredoxin domain carrying a dinuclear electron entry site CuA, an N-terminal seven-bladed propeller domain with the active center CuZ
homodimer
Marinobacter nauticus 617
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2 * 65000, SDS-PAGE
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homodimer
Marinobacter nauticus 617
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2 * 65373, ESI mass spectrometry
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homodimer
Marinobacter nauticus 617
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2 * ?, each monomer is composed of two domains, a C-terminal cupredoxin domain carrying a dinuclear electron entry site CuA, an N-terminal seven-bladed propeller domain with the active center CuZ
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homodimer
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2 * ?, each monomer is composed of two domains, a C-terminal cupredoxin domain carrying a dinuclear electron entry site CuA, an N-terminal seven-bladed propeller domain with the active center CuZ
homodimer
2 * 64810, maturated enzyme, sequence calculation, a homodimer with a distinct two-domain architecture in the protomer
homodimer
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2 * 64810, maturated enzyme, sequence calculation, a homodimer with a distinct two-domain architecture in the protomer
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perturbations of the protein conformation induced by pH variations, although the principal secondary structure elements are largely unaltered
additional information
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perturbations of the protein conformation induced by pH variations, although the principal secondary structure elements are largely unaltered
additional information
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perturbations of the protein conformation induced by pH variations, although the principal secondary structure elements are largely unaltered
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additional information
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the enzyme contains an unusual mixed valence copper, Cu(I)/Cu(II), dimer centre, coherent Raman detected electron spin resonance spectroscopy structure analysis of the CuA site in nitrous oxide reductase, overview
additional information
calcium plays a role in secondary structure stabilization during maturation of nitrous oxide reductase. The enzyme contains a signal peptide with the twin-arginine motif S-RR-S-F-M-G that is required for Tat-dependent translocation to the periplasm. Three-dimensional structure analysis, overview
additional information
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calcium plays a role in secondary structure stabilization during maturation of nitrous oxide reductase. The enzyme contains a signal peptide with the twin-arginine motif S-RR-S-F-M-G that is required for Tat-dependent translocation to the periplasm. Three-dimensional structure analysis, overview
additional information
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calcium plays a role in secondary structure stabilization during maturation of nitrous oxide reductase. The enzyme contains a signal peptide with the twin-arginine motif S-RR-S-F-M-G that is required for Tat-dependent translocation to the periplasm. Three-dimensional structure analysis, overview
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