node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KKO83562.1 | KKO84471.1 | AAV33_05845 | AAV33_00655 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.712 |
KKO83562.1 | KKO84473.1 | AAV33_05845 | AAV33_00665 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.434 |
KKO83562.1 | ctaA | AAV33_05845 | AAV33_00100 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B561; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.898 |
KKO83562.1 | ctaB | AAV33_05845 | AAV33_00095 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; 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. | 0.687 |
KKO83562.1 | ctaD | AAV33_05845 | AAV33_03905 | Membrane 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. | 0.652 |
KKO83562.1 | qcrC | AAV33_05845 | AAV33_00670 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.669 |
KKO84471.1 | KKO83562.1 | AAV33_00655 | AAV33_05845 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.712 |
KKO84471.1 | KKO84473.1 | AAV33_00655 | AAV33_00665 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
KKO84471.1 | ctaA | AAV33_00655 | AAV33_00100 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B561; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.746 |
KKO84471.1 | ctaB | AAV33_00655 | AAV33_00095 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; 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. | 0.998 |
KKO84471.1 | ctaD | AAV33_00655 | AAV33_03905 | 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. | 0.999 |
KKO84471.1 | kgd | AAV33_00655 | AAV33_03165 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Alpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.590 |
KKO84471.1 | qcrB | AAV33_00655 | AAV33_00680 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
KKO84471.1 | qcrC | AAV33_00655 | AAV33_00670 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
KKO84473.1 | KKO83562.1 | AAV33_00665 | AAV33_05845 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.434 |
KKO84473.1 | KKO84471.1 | AAV33_00665 | AAV33_00655 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
KKO84473.1 | ctaA | AAV33_00665 | AAV33_00100 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B561; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.652 |
KKO84473.1 | ctaB | AAV33_00665 | AAV33_00095 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; 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. | 0.999 |
KKO84473.1 | ctaD | AAV33_00665 | AAV33_03905 | 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. | 0.999 |
KKO84473.1 | kgd | AAV33_00665 | AAV33_03165 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Alpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.600 |