| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BAMA_00840 | BAMA_05500 | BAMA_00840 | BAMA_05500 | Derived by automated computational analysis using gene prediction method: Protein Homology. | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| BAMA_00840 | BAMA_09085 | BAMA_00840 | BAMA_09085 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; 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). | 0.994 |
| BAMA_00840 | BAMA_14100 | BAMA_00840 | BAMA_14100 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.962 |
| BAMA_00840 | BAMA_14105 | BAMA_00840 | BAMA_14105 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.982 |
| BAMA_00840 | BAMA_21175 | BAMA_00840 | BAMA_21175 | Derived by automated computational analysis using gene prediction method: Protein Homology. | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.616 |
| BAMA_00840 | nuoD | BAMA_00840 | BAMA_01310 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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 a menaquinone. 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. | 0.562 |
| BAMA_00840 | nuoI | BAMA_00840 | BAMA_01300 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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. | 0.784 |
| BAMA_00840 | sdhB | BAMA_00840 | BAMA_02860 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.757 |
| BAMA_05500 | BAMA_00840 | BAMA_05500 | BAMA_00840 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| BAMA_05500 | BAMA_09085 | BAMA_05500 | BAMA_09085 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; 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). | 0.998 |
| BAMA_05500 | BAMA_14100 | BAMA_05500 | BAMA_14100 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.956 |
| BAMA_05500 | BAMA_14105 | BAMA_05500 | BAMA_14105 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.956 |
| BAMA_05500 | BAMA_21175 | BAMA_05500 | BAMA_21175 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.950 |
| BAMA_05500 | BAMA_22175 | BAMA_05500 | BAMA_22175 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| BAMA_05500 | nuoD | BAMA_05500 | BAMA_01310 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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 a menaquinone. 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. | 0.952 |
| BAMA_05500 | nuoI | BAMA_05500 | BAMA_01300 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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. | 0.957 |
| BAMA_05500 | sdhA | BAMA_05500 | BAMA_02855 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.982 |
| BAMA_05500 | sdhB | BAMA_05500 | BAMA_02860 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.956 |
| BAMA_09085 | BAMA_00840 | BAMA_09085 | BAMA_00840 | Cytochrome B; 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| BAMA_09085 | BAMA_05500 | BAMA_09085 | BAMA_05500 | Cytochrome B; 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). | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
