node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A5784_07930 | A5784_10470 | A5784_07930 | A5784_10470 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | NADH-quinone oxidoreductase subunit K; 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. | 0.999 |
A5784_07930 | A5784_15610 | A5784_07930 | A5784_15610 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Porin; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.999 |
A5784_07930 | A5784_22000 | A5784_07930 | A5784_22000 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | NADH-quinone oxidoreductase subunit H; Incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.999 |
A5784_07930 | OBC02154.1 | A5784_07930 | A5784_16330 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
A5784_07930 | OBC11022.1 | A5784_07930 | A5784_35590 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
A5784_07930 | nuoB | A5784_07930 | A5784_16315 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | NADH dehydrogenase; 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. | 0.999 |
A5784_07930 | nuoC | A5784_07930 | A5784_16320 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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. | 0.999 |
A5784_07930 | nuoD | A5784_07930 | A5784_16325 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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 |
A5784_07930 | nuoN | A5784_07930 | A5784_05645 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; 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 subunit 2 family. | 0.999 |
A5784_07930 | nuoN-2 | A5784_07930 | A5784_07420 | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | NADH-quinone oxidoreductase subunit M; 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 subunit 2 family. | 0.999 |
A5784_10470 | A5784_07930 | A5784_10470 | A5784_07930 | NADH-quinone oxidoreductase subunit K; 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. | Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.999 |
A5784_10470 | A5784_15610 | A5784_10470 | A5784_15610 | NADH-quinone oxidoreductase subunit K; 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. | Porin; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.999 |
A5784_10470 | A5784_22000 | A5784_10470 | A5784_22000 | NADH-quinone oxidoreductase subunit K; 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. | NADH-quinone oxidoreductase subunit H; Incomplete; too short partial abutting assembly gap; missing stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.999 |
A5784_10470 | OBC02154.1 | A5784_10470 | A5784_16330 | NADH-quinone oxidoreductase subunit K; 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. | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
A5784_10470 | OBC11022.1 | A5784_10470 | A5784_35590 | NADH-quinone oxidoreductase subunit K; 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. | NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
A5784_10470 | nuoB | A5784_10470 | A5784_16315 | NADH-quinone oxidoreductase subunit K; 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. | NADH dehydrogenase; 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. | 0.999 |
A5784_10470 | nuoC | A5784_10470 | A5784_16320 | NADH-quinone oxidoreductase subunit K; 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. | 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. | 0.999 |
A5784_10470 | nuoD | A5784_10470 | A5784_16325 | NADH-quinone oxidoreductase subunit K; 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. | 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 |
A5784_10470 | nuoN | A5784_10470 | A5784_05645 | NADH-quinone oxidoreductase subunit K; 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. | Hypothetical protein; 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 subunit 2 family. | 0.999 |
A5784_10470 | nuoN-2 | A5784_10470 | A5784_07420 | NADH-quinone oxidoreductase subunit K; 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. | NADH-quinone oxidoreductase subunit M; 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 subunit 2 family. | 0.999 |