node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFC44559.1 | SFC46805.1 | SAMN05421848_1389 | SAMN05421848_1497 | NADH dehydrogenase subunit M. | Heptosyltransferase-2. | 0.875 |
SFC44559.1 | SFC52980.1 | SAMN05421848_1389 | SAMN05421848_1822 | NADH dehydrogenase subunit M. | Heptosyltransferase-3. | 0.875 |
SFC44559.1 | SFC71609.1 | SAMN05421848_1389 | SAMN05421848_2413 | NADH dehydrogenase subunit M. | Ferredoxin-NADP reductase. | 0.969 |
SFC44559.1 | nuoA | SAMN05421848_1389 | SAMN05421848_1400 | NADH dehydrogenase subunit M. | NADH dehydrogenase subunit A; 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 subunit 3 family. | 0.999 |
SFC44559.1 | nuoB | SAMN05421848_1389 | SAMN05421848_1399 | NADH dehydrogenase subunit M. | NADH dehydrogenase 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. | 0.999 |
SFC44559.1 | nuoC | SAMN05421848_1389 | SAMN05421848_1398 | NADH dehydrogenase subunit M. | NADH dehydrogenase subunit C /NADH dehydrogenase subunit D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
SFC44559.1 | nuoH | SAMN05421848_1389 | SAMN05421848_1394 | NADH dehydrogenase subunit M. | NADH dehydrogenase 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. | 0.999 |
SFC44559.1 | nuoI | SAMN05421848_1389 | SAMN05421848_1393 | NADH dehydrogenase subunit M. | NADH dehydrogenase 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. | 0.999 |
SFC44559.1 | nuoN | SAMN05421848_1389 | SAMN05421848_1388 | NADH dehydrogenase subunit M. | NADH dehydrogenase subunit N; 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 subunit 2 family. | 0.999 |
SFC46646.1 | SFC46805.1 | SAMN05421848_1488 | SAMN05421848_1497 | 3-deoxy-D-manno-octulosonic-acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family. | Heptosyltransferase-2. | 0.959 |
SFC46646.1 | SFC52980.1 | SAMN05421848_1488 | SAMN05421848_1822 | 3-deoxy-D-manno-octulosonic-acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family. | Heptosyltransferase-3. | 0.703 |
SFC46805.1 | SFC44559.1 | SAMN05421848_1497 | SAMN05421848_1389 | Heptosyltransferase-2. | NADH dehydrogenase subunit M. | 0.875 |
SFC46805.1 | SFC46646.1 | SAMN05421848_1497 | SAMN05421848_1488 | Heptosyltransferase-2. | 3-deoxy-D-manno-octulosonic-acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family. | 0.959 |
SFC46805.1 | SFC52980.1 | SAMN05421848_1497 | SAMN05421848_1822 | Heptosyltransferase-2. | Heptosyltransferase-3. | 0.909 |
SFC46805.1 | SFC71609.1 | SAMN05421848_1497 | SAMN05421848_2413 | Heptosyltransferase-2. | Ferredoxin-NADP reductase. | 0.862 |
SFC46805.1 | nuoA | SAMN05421848_1497 | SAMN05421848_1400 | Heptosyltransferase-2. | NADH dehydrogenase subunit A; 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 subunit 3 family. | 0.863 |
SFC46805.1 | nuoB | SAMN05421848_1497 | SAMN05421848_1399 | Heptosyltransferase-2. | NADH dehydrogenase 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. | 0.863 |
SFC46805.1 | nuoC | SAMN05421848_1497 | SAMN05421848_1398 | Heptosyltransferase-2. | NADH dehydrogenase subunit C /NADH dehydrogenase subunit D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.998 |
SFC46805.1 | nuoH | SAMN05421848_1497 | SAMN05421848_1394 | Heptosyltransferase-2. | NADH dehydrogenase 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. | 0.863 |
SFC46805.1 | nuoI | SAMN05421848_1497 | SAMN05421848_1393 | Heptosyltransferase-2. | NADH dehydrogenase 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. | 0.871 |