| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMM92335.1 | AMM95155.1 | UP17_07120 | UP17_24125 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AMM92335.1 | AMM95249.1 | UP17_07120 | UP17_24660 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.995 |
| AMM92335.1 | AMM95717.1 | UP17_07120 | UP17_24670 | 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. | 0.995 |
| AMM92335.1 | atpA | UP17_07120 | UP17_24155 | 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). | ATP F0F1 synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.987 |
| AMM92335.1 | atpH | UP17_07120 | UP17_24160 | 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). | ATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.986 |
| AMM92335.1 | mlpA | UP17_07120 | UP17_08040 | 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. | 0.981 |
| AMM92335.1 | nuoD | UP17_07120 | UP17_24120 | 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. | 0.997 |
| AMM92335.1 | nuoI | UP17_07120 | UP17_24110 | 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 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. | 0.995 |
| AMM92335.1 | sdhB | UP17_07120 | UP17_17855 | 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). | 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. | 0.993 |
| AMM95155.1 | AMM92335.1 | UP17_24125 | UP17_07120 | Hypothetical 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). | 0.997 |
| AMM95155.1 | AMM95249.1 | UP17_24125 | UP17_24660 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.900 |
| AMM95155.1 | AMM95717.1 | UP17_24125 | UP17_24670 | Hypothetical 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. | 0.900 |
| AMM95155.1 | atpA | UP17_24125 | UP17_24155 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP F0F1 synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.924 |
| AMM95155.1 | atpH | UP17_24125 | UP17_24160 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.910 |
| AMM95155.1 | mlpA | UP17_24125 | UP17_08040 | Hypothetical protein; 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. | 0.849 |
| AMM95155.1 | nuoD | UP17_24125 | UP17_24120 | Hypothetical 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. | 0.999 |
| AMM95155.1 | nuoI | UP17_24125 | UP17_24110 | Hypothetical 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. | 0.999 |
| AMM95155.1 | sdhB | UP17_24125 | UP17_17855 | Hypothetical 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. | 0.890 |
| AMM95249.1 | AMM92335.1 | UP17_24660 | UP17_07120 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.995 |
| AMM95249.1 | AMM95155.1 | UP17_24660 | UP17_24125 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
