node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OJV39509.1 | OJV39702.1 | BGO25_01505 | BGO25_00230 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.757 |
OJV39509.1 | OJV39920.1 | BGO25_01505 | BGO25_08905 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.675 |
OJV39509.1 | OJV40983.1 | BGO25_01505 | BGO25_14480 | 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+. | 0.779 |
OJV39509.1 | OJV41249.1 | BGO25_01505 | BGO25_16010 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 4Fe-4S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.775 |
OJV39509.1 | OJV43915.1 | BGO25_01505 | BGO25_12305 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.698 |
OJV39509.1 | OJV44474.1 | BGO25_01505 | BGO25_05125 | 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). | 0.823 |
OJV39509.1 | OJV44480.1 | BGO25_01505 | BGO25_05160 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.801 |
OJV39702.1 | OJV39509.1 | BGO25_00230 | BGO25_01505 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.757 |
OJV39702.1 | OJV39915.1 | BGO25_00230 | BGO25_08875 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.967 |
OJV39702.1 | OJV39920.1 | BGO25_00230 | BGO25_08905 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.867 |
OJV39702.1 | OJV40983.1 | BGO25_00230 | BGO25_14480 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.671 |
OJV39702.1 | OJV41249.1 | BGO25_00230 | BGO25_16010 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 4Fe-4S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.728 |
OJV39702.1 | OJV42407.1 | BGO25_00230 | BGO25_02590 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | GMC family oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.556 |
OJV39702.1 | OJV43915.1 | BGO25_00230 | BGO25_12305 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.757 |
OJV39702.1 | OJV44172.1 | BGO25_00230 | BGO25_13885 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Monooxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.611 |
OJV39702.1 | OJV44474.1 | BGO25_00230 | BGO25_05125 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.967 |
OJV39702.1 | OJV44480.1 | BGO25_00230 | BGO25_05160 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.954 |
OJV39915.1 | OJV39702.1 | BGO25_08875 | BGO25_00230 | 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). | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.967 |
OJV39915.1 | OJV39920.1 | BGO25_08875 | BGO25_08905 | 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). | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
OJV39915.1 | OJV40983.1 | BGO25_08875 | BGO25_14480 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.840 |