node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFY27225.1 | AFY27895.1 | Cyagr_0004 | Cyagr_0707 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | PFAM: Protein of unknown function (DUF2996). | 0.559 |
AFY27225.1 | ndhH | Cyagr_0004 | Cyagr_2851 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH:ubiquinone oxidoreductase 49 kD 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. | 0.837 |
AFY27225.1 | ndhK | Cyagr_0004 | Cyagr_2137 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH-quinone oxidoreductase, B subunit; 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. | 0.442 |
AFY27225.1 | ndhL | Cyagr_0004 | Cyagr_3347 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase transmembrane subunit; 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. | 0.787 |
AFY27225.1 | ndhM | Cyagr_0004 | Cyagr_2889 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Cyanobacterial and plastid NDH-1 subunit M; 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. | 0.745 |
AFY27225.1 | ndhN | Cyagr_0004 | Cyagr_1810 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH-quinone oxidoreductase cyanobacterial subunit N; 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. | 0.745 |
AFY27225.1 | ndhO | Cyagr_0004 | Cyagr_2936 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Cyanobacterial and plant NDH-1 subunit O; 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. | 0.860 |
AFY27530.1 | AFY27895.1 | Cyagr_0336 | Cyagr_0707 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | PFAM: Protein of unknown function (DUF2996). | 0.421 |
AFY27530.1 | ndhH | Cyagr_0336 | Cyagr_2851 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH:ubiquinone oxidoreductase 49 kD 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. | 0.972 |
AFY27530.1 | ndhI | Cyagr_0336 | Cyagr_2874 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH-plastoquinone oxidoreductase subunit I protein; 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; Belongs to the complex I 23 kDa subunit family. | 0.806 |
AFY27530.1 | ndhK | Cyagr_0336 | Cyagr_2137 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH-quinone oxidoreductase, B subunit; 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. | 0.791 |
AFY27530.1 | ndhL | Cyagr_0336 | Cyagr_3347 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase transmembrane subunit; 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. | 0.749 |
AFY27530.1 | ndhM | Cyagr_0336 | Cyagr_2889 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Cyanobacterial and plastid NDH-1 subunit M; 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. | 0.864 |
AFY27530.1 | ndhN | Cyagr_0336 | Cyagr_1810 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH-quinone oxidoreductase cyanobacterial subunit N; 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. | 0.835 |
AFY27530.1 | ndhO | Cyagr_0336 | Cyagr_2936 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Cyanobacterial and plant NDH-1 subunit O; 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. | 0.935 |
AFY27895.1 | AFY27225.1 | Cyagr_0707 | Cyagr_0004 | PFAM: Protein of unknown function (DUF2996). | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.559 |
AFY27895.1 | AFY27530.1 | Cyagr_0707 | Cyagr_0336 | PFAM: Protein of unknown function (DUF2996). | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.421 |
AFY27895.1 | AFY30215.1 | Cyagr_0707 | Cyagr_3135 | PFAM: Protein of unknown function (DUF2996). | Ferredoxin, (2Fe-2S); PFAM: 2Fe-2S iron-sulfur cluster binding domain; TIGRFAM: ferredoxin [2Fe-2S]. | 0.944 |
AFY27895.1 | ndhH | Cyagr_0707 | Cyagr_2851 | PFAM: Protein of unknown function (DUF2996). | NADH:ubiquinone oxidoreductase 49 kD 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. | 0.766 |
AFY27895.1 | ndhI | Cyagr_0707 | Cyagr_2874 | PFAM: Protein of unknown function (DUF2996). | NADH-plastoquinone oxidoreductase subunit I protein; 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; Belongs to the complex I 23 kDa subunit family. | 0.944 |