BRENDA - Enzyme Database

Comparative analysis of amino acid composition in the active site of nirk gene encoding copper-containing nitrite reductase (CuNiR) in bacterial spp

Adhikari, U.K.; Rahman, M.M.; Comput. Biol. Chem. 67, 102-113 (2017)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Tetrasphaera japonica
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Tetrasphaera jenkinsii
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Mesorhizobium plurifarium
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Pseudomonas protegens
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Sinorhizobium fredii
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Shinella sp. DD12
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Bosea sp. LC85
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Azospirillum lipoferum
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Bradyrhizobium oligotrophicum
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Phaeobacter gallaeciensis
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera japonica
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera jenkinsii
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Mesorhizobium plurifarium
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Pseudomonas protegens
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Sinorhizobium fredii
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Shinella sp. DD12
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Bosea sp. LC85
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Azospirillum lipoferum
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Bradyrhizobium oligotrophicum
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Phaeobacter gallaeciensis
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Bradyrhizobium oligotrophicum S58
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Pseudomonas protegens CHA0
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Azospirillum lipoferum 4B
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera japonica T1-X7
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Sinorhizobium fredii USDA 257
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Phaeobacter gallaeciensis 2.10
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera jenkinsii Ben 74
-
nitric oxide + H2O + ferricytochrome c
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.7.2.1
Azospirillum lipoferum
G7ZE78
-
-
1.7.2.1
Azospirillum lipoferum 4B
G7ZE78
-
-
1.7.2.1
Bosea sp. LC85
A0A085FMZ3
-
-
1.7.2.1
Bradyrhizobium oligotrophicum
M4Z2Q6
-
-
1.7.2.1
Bradyrhizobium oligotrophicum S58
M4Z2Q6
-
-
1.7.2.1
Mesorhizobium plurifarium
A0A090F2L3
-
-
1.7.2.1
Phaeobacter gallaeciensis
-
-
-
1.7.2.1
Phaeobacter gallaeciensis 2.10
-
-
-
1.7.2.1
Pseudomonas protegens
A0A2C9EU40
-
-
1.7.2.1
Pseudomonas protegens CHA0
A0A2C9EU40
-
-
1.7.2.1
Shinella sp. DD12
A0A021X0B0
-
-
1.7.2.1
Sinorhizobium fredii
I3X948
-
-
1.7.2.1
Sinorhizobium fredii USDA 257
I3X948
-
-
1.7.2.1
Tetrasphaera japonica
A0A077M3S9
-
-
1.7.2.1
Tetrasphaera japonica T1-X7
A0A077M3S9
-
-
1.7.2.1
Tetrasphaera jenkinsii
A0A077MDD6
-
-
1.7.2.1
Tetrasphaera jenkinsii Ben 74
A0A077MDD6
-
-
Reaction
EC Number
Reaction
Commentary
Organism
Reaction ID
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Tetrasphaera japonica
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Tetrasphaera jenkinsii
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Mesorhizobium plurifarium
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Pseudomonas protegens
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Sinorhizobium fredii
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Shinella sp. DD12
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Bosea sp. LC85
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Azospirillum lipoferum
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Bradyrhizobium oligotrophicum
1.7.2.1
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
Phaeobacter gallaeciensis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera japonica
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera jenkinsii
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Mesorhizobium plurifarium
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Pseudomonas protegens
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Sinorhizobium fredii
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Shinella sp. DD12
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Bosea sp. LC85
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Azospirillum lipoferum
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Bradyrhizobium oligotrophicum
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Phaeobacter gallaeciensis
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Bradyrhizobium oligotrophicum S58
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Pseudomonas protegens CHA0
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Azospirillum lipoferum 4B
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera japonica T1-X7
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Sinorhizobium fredii USDA 257
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Phaeobacter gallaeciensis 2.10
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera jenkinsii Ben 74
nitric oxide + H2O + ferricytochrome c
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Tetrasphaera japonica
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Tetrasphaera jenkinsii
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Mesorhizobium plurifarium
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Pseudomonas protegens
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Sinorhizobium fredii
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Shinella sp. DD12
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Bosea sp. LC85
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Azospirillum lipoferum
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Bradyrhizobium oligotrophicum
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Phaeobacter gallaeciensis
Synonyms
EC Number
Synonyms
Commentary
Organism
1.7.2.1
copper-containing nitrite reductase
-
Tetrasphaera japonica
1.7.2.1
copper-containing nitrite reductase
-
Tetrasphaera jenkinsii
1.7.2.1
copper-containing nitrite reductase
-
Mesorhizobium plurifarium
1.7.2.1
copper-containing nitrite reductase
-
Pseudomonas protegens
1.7.2.1
copper-containing nitrite reductase
-
Sinorhizobium fredii
1.7.2.1
copper-containing nitrite reductase
-
Shinella sp. DD12
1.7.2.1
copper-containing nitrite reductase
-
Bosea sp. LC85
1.7.2.1
copper-containing nitrite reductase
-
Azospirillum lipoferum
1.7.2.1
copper-containing nitrite reductase
-
Bradyrhizobium oligotrophicum
1.7.2.1
copper-containing nitrite reductase
-
Phaeobacter gallaeciensis
1.7.2.1
CuNIR
-
Tetrasphaera japonica
1.7.2.1
CuNIR
-
Tetrasphaera jenkinsii
1.7.2.1
CuNIR
-
Mesorhizobium plurifarium
1.7.2.1
CuNIR
-
Pseudomonas protegens
1.7.2.1
CuNIR
-
Sinorhizobium fredii
1.7.2.1
CuNIR
-
Shinella sp. DD12
1.7.2.1
CuNIR
-
Bosea sp. LC85
1.7.2.1
CuNIR
-
Azospirillum lipoferum
1.7.2.1
CuNIR
-
Bradyrhizobium oligotrophicum
1.7.2.1
CuNIR
-
Phaeobacter gallaeciensis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.7.2.1
cytochrome c
-
Tetrasphaera japonica
1.7.2.1
cytochrome c
-
Tetrasphaera jenkinsii
1.7.2.1
cytochrome c
-
Mesorhizobium plurifarium
1.7.2.1
cytochrome c
-
Pseudomonas protegens
1.7.2.1
cytochrome c
-
Sinorhizobium fredii
1.7.2.1
cytochrome c
-
Shinella sp. DD12
1.7.2.1
cytochrome c
-
Bosea sp. LC85
1.7.2.1
cytochrome c
-
Azospirillum lipoferum
1.7.2.1
cytochrome c
-
Bradyrhizobium oligotrophicum
1.7.2.1
cytochrome c
-
Phaeobacter gallaeciensis
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Tetrasphaera japonica
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Tetrasphaera jenkinsii
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Mesorhizobium plurifarium
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Pseudomonas protegens
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Sinorhizobium fredii
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Shinella sp. DD12
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Bosea sp. LC85
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Azospirillum lipoferum
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Bradyrhizobium oligotrophicum
1.7.2.1
gene nirK, sequence comparisons, and phylogenetic analysis and tree
Phaeobacter gallaeciensis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.7.2.1
cytochrome c
-
Tetrasphaera japonica
1.7.2.1
cytochrome c
-
Tetrasphaera jenkinsii
1.7.2.1
cytochrome c
-
Mesorhizobium plurifarium
1.7.2.1
cytochrome c
-
Pseudomonas protegens
1.7.2.1
cytochrome c
-
Sinorhizobium fredii
1.7.2.1
cytochrome c
-
Shinella sp. DD12
1.7.2.1
cytochrome c
-
Bosea sp. LC85
1.7.2.1
cytochrome c
-
Azospirillum lipoferum
1.7.2.1
cytochrome c
-
Bradyrhizobium oligotrophicum
1.7.2.1
cytochrome c
-
Phaeobacter gallaeciensis
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera japonica
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera jenkinsii
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Mesorhizobium plurifarium
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Pseudomonas protegens
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Sinorhizobium fredii
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Shinella sp. DD12
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Bosea sp. LC85
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Azospirillum lipoferum
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Bradyrhizobium oligotrophicum
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Phaeobacter gallaeciensis
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Bradyrhizobium oligotrophicum S58
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Pseudomonas protegens CHA0
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Azospirillum lipoferum 4B
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera japonica T1-X7
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Sinorhizobium fredii USDA 257
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Phaeobacter gallaeciensis 2.10
-
nitric oxide + H2O + ferricytochrome c
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
Tetrasphaera jenkinsii Ben 74
-
nitric oxide + H2O + ferricytochrome c
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera japonica
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera jenkinsii
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Mesorhizobium plurifarium
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Pseudomonas protegens
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Sinorhizobium fredii
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Shinella sp. DD12
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Bosea sp. LC85
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Azospirillum lipoferum
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Bradyrhizobium oligotrophicum
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Phaeobacter gallaeciensis
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Bradyrhizobium oligotrophicum S58
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Pseudomonas protegens CHA0
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Azospirillum lipoferum 4B
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera japonica T1-X7
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Sinorhizobium fredii USDA 257
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Phaeobacter gallaeciensis 2.10
nitric oxide + H2O + ferricytochrome c
-
-
-
?
1.7.2.1
nitrite + ferrocytochrome c + 2 H+
-
742316
Tetrasphaera jenkinsii Ben 74
nitric oxide + H2O + ferricytochrome c
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Tetrasphaera japonica
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Tetrasphaera jenkinsii
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Mesorhizobium plurifarium
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Pseudomonas protegens
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Sinorhizobium fredii
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Shinella sp. DD12
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Bosea sp. LC85
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Azospirillum lipoferum
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Bradyrhizobium oligotrophicum
1.7.2.1
More
structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure
Phaeobacter gallaeciensis
General Information
EC Number
General Information
Commentary
Organism
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Tetrasphaera japonica
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Tetrasphaera jenkinsii
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Mesorhizobium plurifarium
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Pseudomonas protegens
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Sinorhizobium fredii
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Shinella sp. DD12
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Bosea sp. LC85
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Azospirillum lipoferum
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Bradyrhizobium oligotrophicum
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Phaeobacter gallaeciensis
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Tetrasphaera japonica
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Tetrasphaera jenkinsii
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Mesorhizobium plurifarium
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Pseudomonas protegens
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Sinorhizobium fredii
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Shinella sp. DD12
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Bosea sp. LC85
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Azospirillum lipoferum
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Bradyrhizobium oligotrophicum
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Phaeobacter gallaeciensis
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Tetrasphaera japonica
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Tetrasphaera jenkinsii
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Mesorhizobium plurifarium
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Pseudomonas protegens
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Sinorhizobium fredii
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Shinella sp. DD12
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Bosea sp. LC85
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Azospirillum lipoferum
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Bradyrhizobium oligotrophicum
1.7.2.1
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
Phaeobacter gallaeciensis
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Tetrasphaera japonica
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Tetrasphaera jenkinsii
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Mesorhizobium plurifarium
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Pseudomonas protegens
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Sinorhizobium fredii
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Shinella sp. DD12
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Bosea sp. LC85
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Azospirillum lipoferum
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Bradyrhizobium oligotrophicum
1.7.2.1
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
Phaeobacter gallaeciensis