node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AMK11276.1 | AMK11641.1 | AWY79_09175 | AWY79_11200 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
AMK11276.1 | AMK12617.1 | AWY79_09175 | AWY79_16645 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Prenyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.726 |
AMK11276.1 | AMK12618.1 | AWY79_09175 | AWY79_16650 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; 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). | 0.747 |
AMK11276.1 | AMK12620.1 | AWY79_09175 | AWY79_16660 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.765 |
AMK11276.1 | AMK12621.1 | AWY79_09175 | AWY79_16665 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit I; 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. | 0.761 |
AMK11276.1 | AMK12622.1 | AWY79_09175 | AWY79_16670 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Copper chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.430 |
AMK11276.1 | sucD | AWY79_09175 | AWY79_12300 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. | 0.995 |
AMK11641.1 | AMK11276.1 | AWY79_11200 | AWY79_09175 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
AMK11641.1 | AMK12617.1 | AWY79_11200 | AWY79_16645 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Prenyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.726 |
AMK11641.1 | AMK12618.1 | AWY79_11200 | AWY79_16650 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; 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). | 0.747 |
AMK11641.1 | AMK12620.1 | AWY79_11200 | AWY79_16660 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.765 |
AMK11641.1 | AMK12621.1 | AWY79_11200 | AWY79_16665 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit I; 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. | 0.761 |
AMK11641.1 | AMK12622.1 | AWY79_11200 | AWY79_16670 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Copper chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.430 |
AMK11641.1 | sucD | AWY79_11200 | AWY79_12300 | Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. | 0.995 |
AMK12219.1 | AMK12617.1 | AWY79_14415 | AWY79_16645 | Heme b synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Prenyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.900 |
AMK12616.1 | AMK12617.1 | AWY79_16640 | AWY79_16645 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Prenyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.751 |
AMK12616.1 | AMK12618.1 | AWY79_16640 | AWY79_16650 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; 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). | 0.745 |
AMK12616.1 | AMK12619.1 | AWY79_16640 | AWY79_16655 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome-c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.631 |
AMK12616.1 | AMK12620.1 | AWY79_16640 | AWY79_16660 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |
AMK12616.1 | AMK12621.1 | AWY79_16640 | AWY79_16665 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit I; 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. | 0.619 |