| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KZE44613.1 | KZE47535.1 | AV540_23550 | AV540_19255 | 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 ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | KZE49487.1 | AV540_23550 | AV540_15315 | 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). | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | KZE55489.1 | AV540_23550 | AV540_05395 | 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). | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | nuoB | AV540_23550 | AV540_15295 | 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). | 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. | 0.999 |
| KZE44613.1 | nuoC | AV540_23550 | AV540_15300 | 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). | NADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. | 0.999 |
| KZE44613.1 | nuoD | AV540_23550 | AV540_15305 | 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). | 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. | 0.999 |
| KZE44613.1 | qcrA | AV540_23550 | AV540_05390 | 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). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | qcrC | AV540_23550 | AV540_05400 | 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). | Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | soxA_2 | AV540_23550 | AV540_09745 | 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). | Sarcosine oxidase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | ymxG | AV540_23550 | AV540_08420 | 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). | Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M16 family. | 0.999 |
| KZE47535.1 | KZE44613.1 | AV540_19255 | AV540_23550 | 2Fe-2S ferredoxin; 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). | 0.999 |
| KZE47535.1 | KZE49487.1 | AV540_19255 | AV540_15315 | 2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.990 |
| KZE47535.1 | KZE55489.1 | AV540_19255 | AV540_05395 | 2Fe-2S ferredoxin; 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. | 0.994 |
| KZE47535.1 | nuoB | AV540_19255 | AV540_15295 | 2Fe-2S ferredoxin; 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. | 0.971 |
| KZE47535.1 | nuoC | AV540_19255 | AV540_15300 | 2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. | 0.987 |
| KZE47535.1 | nuoD | AV540_19255 | AV540_15305 | 2Fe-2S ferredoxin; 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. | 0.989 |
| KZE47535.1 | qcrC | AV540_19255 | AV540_05400 | 2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
| KZE47535.1 | soxA_2 | AV540_19255 | AV540_09745 | 2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sarcosine oxidase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.983 |
| KZE47535.1 | ymxG | AV540_19255 | AV540_08420 | 2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M16 family. | 0.977 |
| KZE49487.1 | KZE44613.1 | AV540_15315 | AV540_23550 | NADH dehydrogenase; 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). | 0.999 |
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