node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
nuoH | shn_00870 | shn_07055 | shn_00870 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.535 |
nuoH | shn_00875 | shn_07055 | shn_00875 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.545 |
nuoH | shn_04240 | shn_07055 | shn_04240 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.997 |
nuoH | shn_05350 | shn_07055 | shn_05350 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Subunit A of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved with K+; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
nuoH | shn_07035 | shn_07055 | shn_07035 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
nuoH | shn_09760 | shn_07055 | shn_09760 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Pyruvate dehydrogenase complex E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | 0.410 |
nuoH | shn_17865 | shn_07055 | shn_17865 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.545 |
nuoH | shn_17870 | shn_07055 | shn_17870 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.535 |
nuoH | shn_18655 | shn_07055 | shn_18655 | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. | 0.862 |
putA | shn_00870 | shn_16615 | shn_00870 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.753 |
putA | shn_00875 | shn_16615 | shn_00875 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.644 |
putA | shn_04240 | shn_16615 | shn_04240 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.740 |
putA | shn_09760 | shn_16615 | shn_09760 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Pyruvate dehydrogenase complex E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | 0.415 |
putA | shn_17865 | shn_16615 | shn_17865 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.644 |
putA | shn_17870 | shn_16615 | shn_17870 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.753 |
shn_00870 | nuoH | shn_00870 | shn_07055 | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | 0.535 |
shn_00870 | putA | shn_00870 | shn_16615 | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.753 |
shn_00870 | shn_00875 | shn_00870 | shn_00875 | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
shn_00870 | shn_04240 | shn_00870 | shn_04240 | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.540 |
shn_00870 | shn_05350 | shn_00870 | shn_05350 | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | Subunit A of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved with K+; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.659 |