node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Slin_0114 | Slin_4248 | Slin_0114 | Slin_4248 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | 0.628 |
Slin_0114 | nuoD | Slin_0114 | Slin_5101 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.555 |
Slin_0114 | nuoD-2 | Slin_0114 | Slin_5351 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.555 |
Slin_4248 | Slin_0114 | Slin_4248 | Slin_0114 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | 0.628 |
Slin_4248 | Slin_4249 | Slin_4248 | Slin_4249 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | PFAM: NAD-dependent epimerase/dehydratase; Male sterility domain; 3-beta hydroxysteroid dehydrogenase/isomerase; KEGG: mmw:Mmwyl1_1894 NAD-dependent epimerase/dehydratase. | 0.444 |
Slin_4248 | Slin_4432 | Slin_4248 | Slin_4432 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | 0.800 |
Slin_4248 | nuoD | Slin_4248 | Slin_5101 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.555 |
Slin_4248 | nuoD-2 | Slin_4248 | Slin_5351 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.555 |
Slin_4249 | Slin_4248 | Slin_4249 | Slin_4248 | PFAM: NAD-dependent epimerase/dehydratase; Male sterility domain; 3-beta hydroxysteroid dehydrogenase/isomerase; KEGG: mmw:Mmwyl1_1894 NAD-dependent epimerase/dehydratase. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | 0.444 |
Slin_4432 | Slin_4248 | Slin_4432 | Slin_4248 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | 0.800 |
Slin_4432 | nuoD | Slin_4432 | Slin_5101 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.555 |
Slin_4432 | nuoD-2 | Slin_4432 | Slin_5351 | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.555 |
nuoD | Slin_0114 | Slin_5101 | Slin_0114 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | 0.555 |
nuoD | Slin_4248 | Slin_5101 | Slin_4248 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | 0.555 |
nuoD | Slin_4432 | Slin_5101 | Slin_4432 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | 0.555 |
nuoD | nuoD-2 | Slin_5101 | Slin_5351 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.915 |
nuoD-2 | Slin_0114 | Slin_5351 | Slin_0114 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | 0.555 |
nuoD-2 | Slin_4248 | Slin_5351 | Slin_4248 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: dac:Daci_5784 beta-Ig-H3/fasciclin. | 0.555 |
nuoD-2 | Slin_4432 | Slin_5351 | Slin_4432 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin. | 0.555 |
nuoD-2 | nuoD | Slin_5351 | Slin_5101 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. | 0.915 |