node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACL42989.1 | ACL45253.1 | Cyan7425_0599 | Cyan7425_2912 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | 0.702 |
ACL42989.1 | ACL46601.1 | Cyan7425_0599 | Cyan7425_4288 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | KEGG: ter:Tery_1164 hypothetical protein. | 0.757 |
ACL42989.1 | ACL47309.1 | Cyan7425_0599 | Cyan7425_5012 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | KEGG: amr:AM1_0918 hypothetical protein. | 0.717 |
ACL42989.1 | ndhI | Cyan7425_0599 | Cyan7425_1667 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | NADH-plastoquinone oxidoreductase, I 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; Belongs to the complex I 23 kDa subunit family. | 0.482 |
ACL42989.1 | ndhN | Cyan7425_0599 | Cyan7425_0598 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | NADH dehydrogenase I subunit N, putative; 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. | 0.909 |
ACL45253.1 | ACL42989.1 | Cyan7425_2912 | Cyan7425_0599 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | 0.702 |
ACL45253.1 | ACL46601.1 | Cyan7425_2912 | Cyan7425_4288 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | KEGG: ter:Tery_1164 hypothetical protein. | 0.907 |
ACL45253.1 | ACL47309.1 | Cyan7425_2912 | Cyan7425_5012 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | KEGG: amr:AM1_0918 hypothetical protein. | 0.903 |
ACL45253.1 | ndhA | Cyan7425_2912 | Cyan7425_1666 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | NADH dehydrogenase (quinone); 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. | 0.872 |
ACL45253.1 | ndhH | Cyan7425_2912 | Cyan7425_3394 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | NADH dehydrogenase (quinone); 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 |
ACL45253.1 | ndhI | Cyan7425_2912 | Cyan7425_1667 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | NADH-plastoquinone oxidoreductase, I 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; Belongs to the complex I 23 kDa subunit family. | 0.912 |
ACL45253.1 | ndhJ | Cyan7425_2912 | Cyan7425_4173 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | NADH dehydrogenase (ubiquinone) 30 kDa 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. | 0.964 |
ACL45253.1 | ndhL | Cyan7425_2912 | Cyan7425_3162 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | Conserved hypothetical 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.768 |
ACL45253.1 | ndhN | Cyan7425_2912 | Cyan7425_0598 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | NADH dehydrogenase I subunit N, putative; 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. | 0.970 |
ACL45253.1 | ndhO | Cyan7425_2912 | Cyan7425_2385 | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | Conserved hypothetical 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.936 |
ACL46601.1 | ACL42989.1 | Cyan7425_4288 | Cyan7425_0599 | KEGG: ter:Tery_1164 hypothetical protein. | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: amr:AM1_1652 ferredoxin, 4Fe-4S type. | 0.757 |
ACL46601.1 | ACL45253.1 | Cyan7425_4288 | Cyan7425_2912 | KEGG: ter:Tery_1164 hypothetical protein. | KEGG: amr:AM1_6407 NAD(P)H-quinone oxidoreductase subunit M. | 0.907 |
ACL46601.1 | ACL47309.1 | Cyan7425_4288 | Cyan7425_5012 | KEGG: ter:Tery_1164 hypothetical protein. | KEGG: amr:AM1_0918 hypothetical protein. | 0.957 |
ACL46601.1 | ndhA | Cyan7425_4288 | Cyan7425_1666 | KEGG: ter:Tery_1164 hypothetical protein. | NADH dehydrogenase (quinone); 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. | 0.607 |
ACL46601.1 | ndhH | Cyan7425_4288 | Cyan7425_3394 | KEGG: ter:Tery_1164 hypothetical protein. | NADH dehydrogenase (quinone); 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. | 0.831 |