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Literature summary for 1.7.2.1 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
Search for more literature for 1.7.2.1

Cloned(Commentary)

Cloned (Comment) Organism
gene nirK, sequence comparisons, and phylogenetic analysis and tree Tetrasphaera japonica
gene nirK, sequence comparisons, and phylogenetic analysis and tree Tetrasphaera jenkinsii
gene nirK, sequence comparisons, and phylogenetic analysis and tree Mesorhizobium plurifarium
gene nirK, sequence comparisons, and phylogenetic analysis and tree Pseudomonas protegens
gene nirK, sequence comparisons, and phylogenetic analysis and tree Sinorhizobium fredii
gene nirK, sequence comparisons, and phylogenetic analysis and tree Shinella sp. DD12
gene nirK, sequence comparisons, and phylogenetic analysis and tree Bosea sp. LC85
gene nirK, sequence comparisons, and phylogenetic analysis and tree Azospirillum lipoferum
gene nirK, sequence comparisons, and phylogenetic analysis and tree Bradyrhizobium oligotrophicum
gene nirK, sequence comparisons, and phylogenetic analysis and tree Phaeobacter gallaeciensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrite + ferrocytochrome c + 2 H+ Tetrasphaera japonica
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Tetrasphaera jenkinsii
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Mesorhizobium plurifarium
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Pseudomonas protegens
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Sinorhizobium fredii
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Shinella sp. DD12
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Bosea sp. LC85
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Azospirillum lipoferum
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Bradyrhizobium oligotrophicum
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Phaeobacter gallaeciensis
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Bradyrhizobium oligotrophicum S58
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Pseudomonas protegens CHA0
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Azospirillum lipoferum 4B
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Tetrasphaera japonica T1-X7
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Sinorhizobium fredii USDA 257
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Phaeobacter gallaeciensis 2.10
-
 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+ Tetrasphaera jenkinsii Ben 74
-
 nitric oxide + H2O + ferricytochrome c
-
 ?

Organism

Organism UniProt Comment Textmining
Azospirillum lipoferum G7ZE78
-
-
Azospirillum lipoferum 4B G7ZE78
-
-
Bosea sp. LC85 A0A085FMZ3
-
-
Bradyrhizobium oligotrophicum M4Z2Q6
-
-
Bradyrhizobium oligotrophicum S58 M4Z2Q6
-
-
Mesorhizobium plurifarium A0A090F2L3
-
-
Phaeobacter gallaeciensis
-
-
-
Phaeobacter gallaeciensis 2.10
-
-
-
Pseudomonas protegens A0A2C9EU40
-
-
Pseudomonas protegens CHA0 A0A2C9EU40
-
-
Shinella sp. DD12 A0A021X0B0
-
-
Sinorhizobium fredii I3X948
-
-
Sinorhizobium fredii USDA 257 I3X948
-
-
Tetrasphaera japonica A0A077M3S9
-
-
Tetrasphaera japonica T1-X7 A0A077M3S9
-
-
Tetrasphaera jenkinsii A0A077MDD6
-
-
Tetrasphaera jenkinsii Ben 74 A0A077MDD6
-
-

Reaction

Reaction Comment Organism Reaction ID
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Tetrasphaera japonica
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Tetrasphaera jenkinsii
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Mesorhizobium plurifarium
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Pseudomonas protegens
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Sinorhizobium fredii
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Shinella sp. DD12
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Bosea sp. LC85
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Azospirillum lipoferum
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Bradyrhizobium oligotrophicum
a
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ catalytic mechansim, overview Phaeobacter gallaeciensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + ferrocytochrome c + 2 H+
-
 Tetrasphaera japonica nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Tetrasphaera jenkinsii nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Mesorhizobium plurifarium nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Pseudomonas protegens nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Sinorhizobium fredii nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Shinella sp. DD12 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Bosea sp. LC85 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Azospirillum lipoferum nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Bradyrhizobium oligotrophicum nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Phaeobacter gallaeciensis nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Bradyrhizobium oligotrophicum S58 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Pseudomonas protegens CHA0 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Azospirillum lipoferum 4B nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Tetrasphaera japonica T1-X7 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Sinorhizobium fredii USDA 257 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Phaeobacter gallaeciensis 2.10 nitric oxide + H2O + ferricytochrome c
-
 ?
nitrite + ferrocytochrome c + 2 H+
-
 Tetrasphaera jenkinsii Ben 74 nitric oxide + H2O + ferricytochrome c
-
 ?

Subunits

Subunits Comment Organism
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Tetrasphaera japonica
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Tetrasphaera jenkinsii
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Mesorhizobium plurifarium
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Pseudomonas protegens
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Sinorhizobium fredii
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Shinella sp. DD12
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Bosea sp. LC85
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Azospirillum lipoferum
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Bradyrhizobium oligotrophicum
More structure-based comparative modeling of NirK proteins, evaluation, overview. Comparison and analysis of active sites, multiple domain structure Phaeobacter gallaeciensis

Synonyms

Synonyms Comment Organism
copper-containing nitrite reductase
-
 Tetrasphaera japonica
copper-containing nitrite reductase
-
 Tetrasphaera jenkinsii
copper-containing nitrite reductase
-
 Mesorhizobium plurifarium
copper-containing nitrite reductase
-
 Pseudomonas protegens
copper-containing nitrite reductase
-
 Sinorhizobium fredii
copper-containing nitrite reductase
-
 Shinella sp. DD12
copper-containing nitrite reductase
-
 Bosea sp. LC85
copper-containing nitrite reductase
-
 Azospirillum lipoferum
copper-containing nitrite reductase
-
 Bradyrhizobium oligotrophicum
copper-containing nitrite reductase
-
 Phaeobacter gallaeciensis
CuNIR
-
 Tetrasphaera japonica
CuNIR
-
 Tetrasphaera jenkinsii
CuNIR
-
 Mesorhizobium plurifarium
CuNIR
-
 Pseudomonas protegens
CuNIR
-
 Sinorhizobium fredii
CuNIR
-
 Shinella sp. DD12
CuNIR
-
 Bosea sp. LC85
CuNIR
-
 Azospirillum lipoferum
CuNIR
-
 Bradyrhizobium oligotrophicum
CuNIR
-
 Phaeobacter gallaeciensis

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
 Tetrasphaera japonica
cytochrome c
-
 Tetrasphaera jenkinsii
cytochrome c
-
 Mesorhizobium plurifarium
cytochrome c
-
 Pseudomonas protegens
cytochrome c
-
 Sinorhizobium fredii
cytochrome c
-
 Shinella sp. DD12
cytochrome c
-
 Bosea sp. LC85
cytochrome c
-
 Azospirillum lipoferum
cytochrome c
-
 Bradyrhizobium oligotrophicum
cytochrome c
-
 Phaeobacter gallaeciensis

General Information

General Information Comment Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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