node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SKB28688.1 | SKB37614.1 | SAMN05661099_0189 | SAMN05661099_0974 | NADH-quinone oxidoreductase subunit M. | Cytochrome b6-f complex iron-sulfur subunit. | 0.922 |
SKB28688.1 | SKB65225.1 | SAMN05661099_0189 | SAMN05661099_2088 | NADH-quinone oxidoreductase subunit M. | Cytochrome c oxidase subunit 3. | 0.957 |
SKB28688.1 | SKB65242.1 | SAMN05661099_0189 | SAMN05661099_2089 | NADH-quinone oxidoreductase subunit M. | Cytochrome c oxidase subunit 3. | 0.946 |
SKB28688.1 | SKB65293.1 | SAMN05661099_0189 | SAMN05661099_2092 | NADH-quinone oxidoreductase subunit M. | Cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. | 0.990 |
SKB28688.1 | SKB65307.1 | SAMN05661099_0189 | SAMN05661099_2093 | NADH-quinone oxidoreductase subunit M. | Cytochrome c oxidase subunit 2; 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). | 0.982 |
SKB28688.1 | SKB67511.1 | SAMN05661099_0189 | SAMN05661099_2175 | NADH-quinone oxidoreductase subunit M. | NADH-quinone oxidoreductase subunit M. | 0.839 |
SKB28688.1 | nuoH | SAMN05661099_0189 | SAMN05661099_0184 | NADH-quinone oxidoreductase subunit M. | 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. | 0.999 |
SKB28688.1 | nuoH-2 | SAMN05661099_0189 | SAMN05661099_2180 | NADH-quinone oxidoreductase subunit M. | 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. | 0.999 |
SKB37614.1 | SKB28688.1 | SAMN05661099_0974 | SAMN05661099_0189 | Cytochrome b6-f complex iron-sulfur subunit. | NADH-quinone oxidoreductase subunit M. | 0.922 |
SKB37614.1 | SKB65225.1 | SAMN05661099_0974 | SAMN05661099_2088 | Cytochrome b6-f complex iron-sulfur subunit. | Cytochrome c oxidase subunit 3. | 0.975 |
SKB37614.1 | SKB65242.1 | SAMN05661099_0974 | SAMN05661099_2089 | Cytochrome b6-f complex iron-sulfur subunit. | Cytochrome c oxidase subunit 3. | 0.975 |
SKB37614.1 | SKB65293.1 | SAMN05661099_0974 | SAMN05661099_2092 | Cytochrome b6-f complex iron-sulfur subunit. | Cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. | 0.984 |
SKB37614.1 | SKB65307.1 | SAMN05661099_0974 | SAMN05661099_2093 | Cytochrome b6-f complex iron-sulfur subunit. | Cytochrome c oxidase subunit 2; 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). | 0.977 |
SKB37614.1 | SKB67511.1 | SAMN05661099_0974 | SAMN05661099_2175 | Cytochrome b6-f complex iron-sulfur subunit. | NADH-quinone oxidoreductase subunit M. | 0.922 |
SKB37614.1 | SKB94685.1 | SAMN05661099_0974 | SAMN05661099_3640 | Cytochrome b6-f complex iron-sulfur subunit. | Uncharacterized protein. | 0.952 |
SKB37614.1 | nuoH | SAMN05661099_0974 | SAMN05661099_0184 | Cytochrome b6-f complex iron-sulfur subunit. | 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. | 0.924 |
SKB37614.1 | nuoH-2 | SAMN05661099_0974 | SAMN05661099_2180 | Cytochrome b6-f complex iron-sulfur subunit. | 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. | 0.924 |
SKB65225.1 | SKB28688.1 | SAMN05661099_2088 | SAMN05661099_0189 | Cytochrome c oxidase subunit 3. | NADH-quinone oxidoreductase subunit M. | 0.957 |
SKB65225.1 | SKB37614.1 | SAMN05661099_2088 | SAMN05661099_0974 | Cytochrome c oxidase subunit 3. | Cytochrome b6-f complex iron-sulfur subunit. | 0.975 |
SKB65225.1 | SKB65242.1 | SAMN05661099_2088 | SAMN05661099_2089 | Cytochrome c oxidase subunit 3. | Cytochrome c oxidase subunit 3. | 0.981 |