node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFT48094.1 | SFT48104.1 | SAMN04487904_102406 | SAMN04487904_102407 | Multicomponent Na+:H+ antiporter subunit A. | Multicomponent Na+:H+ antiporter subunit B. | 0.999 |
SFT48094.1 | SFT48117.1 | SAMN04487904_102406 | SAMN04487904_102408 | Multicomponent Na+:H+ antiporter subunit A. | Multicomponent Na+:H+ antiporter subunit C. | 0.999 |
SFT48094.1 | SFT48129.1 | SAMN04487904_102406 | SAMN04487904_102409 | Multicomponent Na+:H+ antiporter subunit A. | Multisubunit sodium/proton antiporter, MrpD subunit (TC 2.A.63.1). | 0.999 |
SFT48094.1 | SFT48144.1 | SAMN04487904_102406 | SAMN04487904_102410 | Multicomponent Na+:H+ antiporter subunit A. | Multicomponent Na+:H+ antiporter subunit E. | 0.999 |
SFT48094.1 | SFT48154.1 | SAMN04487904_102406 | SAMN04487904_102411 | Multicomponent Na+:H+ antiporter subunit A. | Multisubunit sodium/proton antiporter, MrpF subunit (TC 2.A.63.1). | 0.999 |
SFT48094.1 | SFT48166.1 | SAMN04487904_102406 | SAMN04487904_102412 | Multicomponent Na+:H+ antiporter subunit A. | Multicomponent Na+:H+ antiporter subunit G. | 0.999 |
SFT48094.1 | SFT59634.1 | SAMN04487904_102406 | SAMN04487904_104144 | Multicomponent Na+:H+ antiporter subunit A. | NADH-quinone oxidoreductase subunit L. | 0.921 |
SFT48094.1 | nuoC | SAMN04487904_102406 | SAMN04487904_104153 | Multicomponent Na+:H+ antiporter subunit A. | NADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. | 0.998 |
SFT48094.1 | nuoD | SAMN04487904_102406 | SAMN04487904_104152 | Multicomponent Na+:H+ antiporter subunit A. | 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 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. | 0.999 |
SFT48094.1 | nuoI | SAMN04487904_102406 | SAMN04487904_104147 | Multicomponent Na+:H+ antiporter subunit A. | 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 |
SFT48104.1 | SFT48094.1 | SAMN04487904_102407 | SAMN04487904_102406 | Multicomponent Na+:H+ antiporter subunit B. | Multicomponent Na+:H+ antiporter subunit A. | 0.999 |
SFT48104.1 | SFT48117.1 | SAMN04487904_102407 | SAMN04487904_102408 | Multicomponent Na+:H+ antiporter subunit B. | Multicomponent Na+:H+ antiporter subunit C. | 0.999 |
SFT48104.1 | SFT48129.1 | SAMN04487904_102407 | SAMN04487904_102409 | Multicomponent Na+:H+ antiporter subunit B. | Multisubunit sodium/proton antiporter, MrpD subunit (TC 2.A.63.1). | 0.999 |
SFT48104.1 | SFT48144.1 | SAMN04487904_102407 | SAMN04487904_102410 | Multicomponent Na+:H+ antiporter subunit B. | Multicomponent Na+:H+ antiporter subunit E. | 0.997 |
SFT48104.1 | SFT48154.1 | SAMN04487904_102407 | SAMN04487904_102411 | Multicomponent Na+:H+ antiporter subunit B. | Multisubunit sodium/proton antiporter, MrpF subunit (TC 2.A.63.1). | 0.983 |
SFT48104.1 | SFT48166.1 | SAMN04487904_102407 | SAMN04487904_102412 | Multicomponent Na+:H+ antiporter subunit B. | Multicomponent Na+:H+ antiporter subunit G. | 0.997 |
SFT48104.1 | SFT59634.1 | SAMN04487904_102407 | SAMN04487904_104144 | Multicomponent Na+:H+ antiporter subunit B. | NADH-quinone oxidoreductase subunit L. | 0.990 |
SFT48104.1 | nuoC | SAMN04487904_102407 | SAMN04487904_104153 | Multicomponent Na+:H+ antiporter subunit B. | NADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. | 0.542 |
SFT48104.1 | nuoD | SAMN04487904_102407 | SAMN04487904_104152 | Multicomponent Na+:H+ antiporter subunit B. | 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 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. | 0.542 |
SFT48104.1 | nuoI | SAMN04487904_102407 | SAMN04487904_104147 | Multicomponent Na+:H+ antiporter subunit B. | 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. | 0.812 |