| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ARE84104.1 | hpnR | ROSMUCSMR3_02635 | ROSMUCSMR3_02636 | V4R domain protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hopanoid C-3 methylase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.999 |
| ARE84104.1 | menH | ROSMUCSMR3_02635 | ROSMUCSMR3_01331 | V4R domain protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.769 |
| acpS | menH | ROSMUCSMR3_01330 | ROSMUCSMR3_01331 | Holo-[acyl-carrier-protein] synthase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.799 |
| acpS | pdxJ | ROSMUCSMR3_01330 | ROSMUCSMR3_01332 | Holo-[acyl-carrier-protein] synthase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. | Pyridoxine 5'-phosphate synthase; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. | 0.864 |
| hpnR | ARE84104.1 | ROSMUCSMR3_02636 | ROSMUCSMR3_02635 | Hopanoid C-3 methylase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | V4R domain protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.999 |
| hpnR | menH | ROSMUCSMR3_02636 | ROSMUCSMR3_01331 | Hopanoid C-3 methylase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.762 |
| menH | ARE84104.1 | ROSMUCSMR3_01331 | ROSMUCSMR3_02635 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | V4R domain protein; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.769 |
| menH | acpS | ROSMUCSMR3_01331 | ROSMUCSMR3_01330 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Holo-[acyl-carrier-protein] synthase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. | 0.799 |
| menH | hpnR | ROSMUCSMR3_01331 | ROSMUCSMR3_02636 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Hopanoid C-3 methylase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.762 |
| menH | nqo1-2 | ROSMUCSMR3_01331 | ROSMUCSMR3_03671 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase subunit 1; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.970 |
| menH | nqo3 | ROSMUCSMR3_01331 | ROSMUCSMR3_00224 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.838 |
| menH | nqo5 | ROSMUCSMR3_01331 | ROSMUCSMR3_00236 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase chain 5; 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; Belongs to the complex I 30 kDa subunit family. | 0.757 |
| menH | nuoB | ROSMUCSMR3_01331 | ROSMUCSMR3_00237 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase subunit B; 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. | 0.772 |
| menH | nuoH | ROSMUCSMR3_01331 | ROSMUCSMR3_00222 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase subunit H; 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. This subunit may bind ubiquinone. | 0.732 |
| menH | nuoI | ROSMUCSMR3_01331 | ROSMUCSMR3_00221 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase subunit I; 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. | 0.771 |
| menH | pdxJ | ROSMUCSMR3_01331 | ROSMUCSMR3_01332 | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | Pyridoxine 5'-phosphate synthase; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. | 0.740 |
| nqo1-2 | menH | ROSMUCSMR3_03671 | ROSMUCSMR3_01331 | NADH-quinone oxidoreductase subunit 1; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | 0.970 |
| nqo1-2 | nqo3 | ROSMUCSMR3_03671 | ROSMUCSMR3_00224 | NADH-quinone oxidoreductase subunit 1; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.998 |
| nqo1-2 | nqo5 | ROSMUCSMR3_03671 | ROSMUCSMR3_00236 | NADH-quinone oxidoreductase subunit 1; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase chain 5; 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; Belongs to the complex I 30 kDa subunit family. | 0.996 |
| nqo1-2 | nuoB | ROSMUCSMR3_03671 | ROSMUCSMR3_00237 | NADH-quinone oxidoreductase subunit 1; Bacteria and source DNA available from Adrian K. Clarke, Department of Biological and Environmental Sciences, University of Gothenburg. | NADH-quinone oxidoreductase subunit B; 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. | 0.996 |