| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BF49_1629 | BF49_1630 | BF49_1629 | BF49_1630 | FIG069766 hypothetical protein. | FIG050708 hypothetical protein. | 0.768 |
| BF49_1630 | BF49_1629 | BF49_1630 | BF49_1629 | FIG050708 hypothetical protein. | FIG069766 hypothetical protein. | 0.768 |
| BF49_1630 | BF49_2624 | BF49_1630 | BF49_2624 | FIG050708 hypothetical protein. | Tungstencontaining formate dehydrogenase beta subunit. | 0.559 |
| BF49_1630 | BF49_5272 | BF49_1630 | BF49_5272 | FIG050708 hypothetical protein. | Cytochrome c oxidase polypeptide III EC 1931. | 0.541 |
| BF49_1630 | BF49_5273 | BF49_1630 | BF49_5273 | FIG050708 hypothetical protein. | Cytochrome c oxidase polypeptide I EC 1931; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.541 |
| BF49_1630 | BF49_6651 | BF49_1630 | BF49_6651 | FIG050708 hypothetical protein. | NADHubiquinone oxidoreductase chain M EC 1653. | 0.556 |
| BF49_1630 | nuoB | BF49_1630 | BF49_5286 | FIG050708 hypothetical protein. | NADHubiquinone oxidoreductase chain B EC 1653; 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. | 0.530 |
| BF49_1630 | nuoB-2 | BF49_1630 | BF49_6638 | FIG050708 hypothetical protein. | NADHubiquinone oxidoreductase chain B EC 1653; 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. | 0.530 |
| BF49_1630 | nuoC | BF49_1630 | BF49_6639 | FIG050708 hypothetical protein. | NADHubiquinone oxidoreductase chain C EC 1653; 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; Belongs to the complex I 30 kDa subunit family. | 0.550 |
| BF49_1630 | nuoD | BF49_1630 | BF49_6640 | FIG050708 hypothetical protein. | NADHubiquinone oxidoreductase chain D EC 1653; 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; Belongs to the complex I 49 kDa subunit family. | 0.541 |
| BF49_1630 | nuoN | BF49_1630 | BF49_6652 | FIG050708 hypothetical protein. | NADHubiquinone oxidoreductase chain N EC 1653; 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; Belongs to the complex I subunit 2 family. | 0.589 |
| BF49_2624 | BF49_1630 | BF49_2624 | BF49_1630 | Tungstencontaining formate dehydrogenase beta subunit. | FIG050708 hypothetical protein. | 0.559 |
| BF49_2624 | BF49_5272 | BF49_2624 | BF49_5272 | Tungstencontaining formate dehydrogenase beta subunit. | Cytochrome c oxidase polypeptide III EC 1931. | 0.980 |
| BF49_2624 | BF49_5273 | BF49_2624 | BF49_5273 | Tungstencontaining formate dehydrogenase beta subunit. | Cytochrome c oxidase polypeptide I EC 1931; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.980 |
| BF49_2624 | BF49_6651 | BF49_2624 | BF49_6651 | Tungstencontaining formate dehydrogenase beta subunit. | NADHubiquinone oxidoreductase chain M EC 1653. | 0.994 |
| BF49_2624 | nuoB | BF49_2624 | BF49_5286 | Tungstencontaining formate dehydrogenase beta subunit. | NADHubiquinone oxidoreductase chain B EC 1653; 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. | 0.993 |
| BF49_2624 | nuoB-2 | BF49_2624 | BF49_6638 | Tungstencontaining formate dehydrogenase beta subunit. | NADHubiquinone oxidoreductase chain B EC 1653; 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. | 0.993 |
| BF49_2624 | nuoC | BF49_2624 | BF49_6639 | Tungstencontaining formate dehydrogenase beta subunit. | NADHubiquinone oxidoreductase chain C EC 1653; 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; Belongs to the complex I 30 kDa subunit family. | 0.995 |
| BF49_2624 | nuoD | BF49_2624 | BF49_6640 | Tungstencontaining formate dehydrogenase beta subunit. | NADHubiquinone oxidoreductase chain D EC 1653; 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; Belongs to the complex I 49 kDa subunit family. | 0.995 |
| BF49_2624 | nuoN | BF49_2624 | BF49_6652 | Tungstencontaining formate dehydrogenase beta subunit. | NADHubiquinone oxidoreductase chain N EC 1653; 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; Belongs to the complex I subunit 2 family. | 0.994 |