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Literature summary extracted from

  • Adhikari, U.K.; Rahman, M.M.
    Comparative analysis of amino acid composition in the active site of nirk gene encoding copper-containing nitrite reductase (CuNiR) in bacterial spp (2017), Comput. Biol. Chem., 67, 102-113 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Comment 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 Comment Organism Reaction ID
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Tetrasphaera japonica
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Tetrasphaera jenkinsii
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Mesorhizobium plurifarium
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Pseudomonas protegens
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Sinorhizobium fredii
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Shinella sp. DD12
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Bosea sp. LC85
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Azospirillum lipoferum
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Bradyrhizobium oligotrophicum
a
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Phaeobacter gallaeciensis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?

Subunits

EC Number Subunits Comment 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 Comment 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 Comment 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

General Information

EC Number General Information Comment 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