| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cce_0546 | cce_3077 | cce_0546 | cce_3077 | Hypothetical protein; Contains a thioredoxin fold domain. | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | 0.970 |
| cce_0546 | hoxF | cce_0546 | cce_2318 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase I chain F. | 0.982 |
| cce_0546 | hoxU | cce_0546 | cce_2317 | Hypothetical protein; Contains a thioredoxin fold domain. | Hydrogenase chain U. | 0.979 |
| cce_0546 | ndhA | cce_0546 | cce_2224 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit 1; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | 0.967 |
| cce_0546 | ndhC | cce_0546 | cce_1764 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit 3; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.964 |
| cce_0546 | ndhE | cce_0546 | cce_2221 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit 4L; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.946 |
| cce_0546 | ndhG | cce_0546 | cce_2222 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit 6; 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 subunit 6 family. | 0.951 |
| cce_0546 | ndhH | cce_0546 | cce_4717 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit 7; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.960 |
| cce_0546 | ndhJ | cce_0546 | cce_1762 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.960 |
| cce_0546 | ndhK | cce_0546 | cce_1763 | Hypothetical protein; Contains a thioredoxin fold domain. | NADH dehydrogenase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. | 0.960 |
| cce_3077 | cce_0546 | cce_3077 | cce_0546 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | Hypothetical protein; Contains a thioredoxin fold domain. | 0.970 |
| cce_3077 | hoxF | cce_3077 | cce_2318 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | NADH dehydrogenase I chain F. | 0.999 |
| cce_3077 | hoxU | cce_3077 | cce_2317 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | Hydrogenase chain U. | 0.988 |
| cce_3077 | ndhA | cce_3077 | cce_2224 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | NADH dehydrogenase subunit 1; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | 0.898 |
| cce_3077 | ndhC | cce_3077 | cce_1764 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | NADH dehydrogenase subunit 3; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.907 |
| cce_3077 | ndhH | cce_3077 | cce_4717 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | NADH dehydrogenase subunit 7; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.992 |
| cce_3077 | ndhJ | cce_3077 | cce_1762 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | NADH dehydrogenase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.994 |
| cce_3077 | ndhK | cce_3077 | cce_1763 | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | NADH dehydrogenase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. | 0.990 |
| hoxF | cce_0546 | cce_2318 | cce_0546 | NADH dehydrogenase I chain F. | Hypothetical protein; Contains a thioredoxin fold domain. | 0.982 |
| hoxF | cce_3077 | cce_2318 | cce_3077 | NADH dehydrogenase I chain F. | AMP-dependent synthetase and ligase, probable acyl-CoA synthase. | 0.999 |