| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EHA62356.1 | EHA63329.1 | Syn8016DRAFT_1651 | Syn8016DRAFT_0370 | KEGG: pme:NATL1_20551 hypothetical protein. | KEGG: pmt:PMT0769 hypothetical protein. | 0.999 |
| EHA62356.1 | ndhB | Syn8016DRAFT_1651 | Syn8016DRAFT_1354 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase subunit 2; 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. | 0.920 |
| EHA62356.1 | ndhC | Syn8016DRAFT_1651 | Syn8016DRAFT_1604 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase 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. | 0.920 |
| EHA62356.1 | ndhE | Syn8016DRAFT_1651 | Syn8016DRAFT_1866 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase 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. | 0.920 |
| EHA62356.1 | ndhI | Syn8016DRAFT_1651 | Syn8016DRAFT_1868 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase subunit I; 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. | 0.999 |
| EHA62356.1 | ndhJ | Syn8016DRAFT_1651 | Syn8016DRAFT_1602 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase 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. | 0.775 |
| EHA62356.1 | ndhK | Syn8016DRAFT_1651 | Syn8016DRAFT_1603 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase 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. | 0.922 |
| EHA62356.1 | ndhM | Syn8016DRAFT_1651 | Syn8016DRAFT_1852 | KEGG: pme:NATL1_20551 hypothetical protein. | NAD(P)H-quinone oxidoreductase 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. | 0.981 |
| EHA62471.1 | EHA62472.1 | Syn8016DRAFT_1766 | Syn8016DRAFT_1767 | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | 0.999 |
| EHA62471.1 | ndhB | Syn8016DRAFT_1766 | Syn8016DRAFT_1354 | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | NAD(P)H-quinone oxidoreductase subunit 2; 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. | 0.999 |
| EHA62471.1 | ndhC | Syn8016DRAFT_1766 | Syn8016DRAFT_1604 | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | NAD(P)H-quinone oxidoreductase 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. | 0.999 |
| EHA62471.1 | ndhI | Syn8016DRAFT_1766 | Syn8016DRAFT_1868 | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | NAD(P)H-quinone oxidoreductase subunit I; 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. | 0.999 |
| EHA62471.1 | ndhJ | Syn8016DRAFT_1766 | Syn8016DRAFT_1602 | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | NAD(P)H-quinone oxidoreductase 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. | 0.999 |
| EHA62471.1 | ndhK | Syn8016DRAFT_1766 | Syn8016DRAFT_1603 | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | NAD(P)H-quinone oxidoreductase 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. | 0.999 |
| EHA62472.1 | EHA62471.1 | Syn8016DRAFT_1767 | Syn8016DRAFT_1766 | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain. | 0.999 |
| EHA62472.1 | ndhB | Syn8016DRAFT_1767 | Syn8016DRAFT_1354 | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | NAD(P)H-quinone oxidoreductase subunit 2; 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. | 0.999 |
| EHA62472.1 | ndhC | Syn8016DRAFT_1767 | Syn8016DRAFT_1604 | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | NAD(P)H-quinone oxidoreductase 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. | 0.999 |
| EHA62472.1 | ndhI | Syn8016DRAFT_1767 | Syn8016DRAFT_1868 | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | NAD(P)H-quinone oxidoreductase subunit I; 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. | 0.999 |
| EHA62472.1 | ndhJ | Syn8016DRAFT_1767 | Syn8016DRAFT_1602 | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | NAD(P)H-quinone oxidoreductase 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. | 0.999 |
| EHA62472.1 | ndhK | Syn8016DRAFT_1767 | Syn8016DRAFT_1603 | KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR. | NAD(P)H-quinone oxidoreductase 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. | 0.999 |