| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KLV05736.1 | KLV05738.1 | ABT57_21195 | ABT57_21210 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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 |
| KLV05736.1 | KLV06365.1 | ABT57_21195 | ABT57_19725 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.821 |
| KLV05736.1 | KLV06366.1 | ABT57_21195 | ABT57_19730 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.984 |
| KLV05736.1 | KLV06367.1 | ABT57_21195 | ABT57_19735 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ubiquinol-cytochrome C reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.964 |
| KLV05736.1 | KLV07942.1 | ABT57_21195 | ABT57_13895 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome P460; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.868 |
| KLV05736.1 | KLV08207.1 | ABT57_21195 | ABT57_15525 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sarcosine oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.775 |
| KLV05736.1 | KLV08286.1 | ABT57_21195 | ABT57_16005 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B558 subunit A; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
| KLV05736.1 | KLV09487.1 | ABT57_21195 | ABT57_11860 | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.868 |
| KLV05736.1 | sdhB | ABT57_21195 | ABT57_23835 | MFS transporter; 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. | 0.658 |
| KLV05738.1 | KLV05736.1 | ABT57_21210 | ABT57_21195 | Cytochrome B559 subunit alpha; 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). | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KLV05738.1 | KLV06097.1 | ABT57_21210 | ABT57_20280 | Cytochrome B559 subunit alpha; 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.867 |
| KLV05738.1 | KLV06365.1 | ABT57_21210 | ABT57_19725 | Cytochrome B559 subunit alpha; 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.954 |
| KLV05738.1 | KLV06366.1 | ABT57_21210 | ABT57_19730 | Cytochrome B559 subunit alpha; 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 B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.999 |
| KLV05738.1 | KLV06367.1 | ABT57_21210 | ABT57_19735 | Cytochrome B559 subunit alpha; 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). | Ubiquinol-cytochrome C reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.997 |
| KLV05738.1 | KLV07942.1 | ABT57_21210 | ABT57_13895 | Cytochrome B559 subunit alpha; 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 P460; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.756 |
| KLV05738.1 | KLV08207.1 | ABT57_21210 | ABT57_15525 | Cytochrome B559 subunit alpha; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.923 |
| KLV05738.1 | KLV08286.1 | ABT57_21210 | ABT57_16005 | Cytochrome B559 subunit alpha; 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 B558 subunit A; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| KLV05738.1 | KLV09487.1 | ABT57_21210 | ABT57_11860 | Cytochrome B559 subunit alpha; 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 Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.773 |
| KLV05738.1 | sdhB | ABT57_21210 | ABT57_23835 | Cytochrome B559 subunit alpha; 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. | 0.908 |
| KLV06097.1 | KLV05738.1 | ABT57_20280 | ABT57_21210 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.867 |
