| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EHA59352.1 | EHA62420.1 | Syn8016DRAFT_2722 | Syn8016DRAFT_1715 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | Capsular exopolysaccharide family; TIGRFAM: Exopolysaccharide synthesis protein; KEGG: pmc:P9515_13861 hypothetical protein; PFAM: Lipopolysaccharide biosynthesis. | 0.529 |
| EHA59352.1 | EHA62471.1 | Syn8016DRAFT_2722 | Syn8016DRAFT_1766 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 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. | 0.430 |
| EHA59352.1 | EHA63429.1 | Syn8016DRAFT_2722 | Syn8016DRAFT_0470 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | 0.627 |
| EHA59352.1 | EHA63463.1 | Syn8016DRAFT_2722 | Syn8016DRAFT_0504 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | PFAM: Protein of unknown function DUF185; KEGG: pmf:P9303_15581 hypothetical protein. | 0.824 |
| EHA59352.1 | ndhH | Syn8016DRAFT_2722 | Syn8016DRAFT_1892 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | NAD(P)H-quinone oxidoreductase subunit H; 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. | 0.865 |
| EHA59352.1 | ndhI | Syn8016DRAFT_2722 | Syn8016DRAFT_1868 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 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. | 0.627 |
| EHA59352.1 | ndhJ | Syn8016DRAFT_2722 | Syn8016DRAFT_1602 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 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. | 0.846 |
| EHA59352.1 | ndhK | Syn8016DRAFT_2722 | Syn8016DRAFT_1603 | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 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. | 0.847 |
| EHA61778.1 | EHA62471.1 | Syn8016DRAFT_1850 | Syn8016DRAFT_1766 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | 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. | 0.747 |
| EHA61778.1 | EHA63429.1 | Syn8016DRAFT_1850 | Syn8016DRAFT_0470 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | 0.757 |
| EHA61778.1 | EHA63463.1 | Syn8016DRAFT_1850 | Syn8016DRAFT_0504 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | PFAM: Protein of unknown function DUF185; KEGG: pmf:P9303_15581 hypothetical protein. | 0.856 |
| EHA61778.1 | ndhH | Syn8016DRAFT_1850 | Syn8016DRAFT_1892 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | NAD(P)H-quinone oxidoreductase subunit H; 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. | 0.851 |
| EHA61778.1 | ndhI | Syn8016DRAFT_1850 | Syn8016DRAFT_1868 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | 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. | 0.757 |
| EHA61778.1 | ndhJ | Syn8016DRAFT_1850 | Syn8016DRAFT_1602 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | 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. | 0.876 |
| EHA61778.1 | ndhK | Syn8016DRAFT_1850 | Syn8016DRAFT_1603 | Phytoene synthase; KEGG: pmj:P9211_01581 squalene and phytoene synthase; PFAM: Squalene/phytoene synthase. | 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. | 0.846 |
| EHA62420.1 | EHA59352.1 | Syn8016DRAFT_1715 | Syn8016DRAFT_2722 | Capsular exopolysaccharide family; TIGRFAM: Exopolysaccharide synthesis protein; KEGG: pmc:P9515_13861 hypothetical protein; PFAM: Lipopolysaccharide biosynthesis. | ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.529 |
| EHA62420.1 | EHA62471.1 | Syn8016DRAFT_1715 | Syn8016DRAFT_1766 | Capsular exopolysaccharide family; TIGRFAM: Exopolysaccharide synthesis protein; KEGG: pmc:P9515_13861 hypothetical protein; PFAM: Lipopolysaccharide biosynthesis. | 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. | 0.574 |
| EHA62420.1 | EHA63429.1 | Syn8016DRAFT_1715 | Syn8016DRAFT_0470 | Capsular exopolysaccharide family; TIGRFAM: Exopolysaccharide synthesis protein; KEGG: pmc:P9515_13861 hypothetical protein; PFAM: Lipopolysaccharide biosynthesis. | 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | 0.680 |
| EHA62420.1 | EHA63463.1 | Syn8016DRAFT_1715 | Syn8016DRAFT_0504 | Capsular exopolysaccharide family; TIGRFAM: Exopolysaccharide synthesis protein; KEGG: pmc:P9515_13861 hypothetical protein; PFAM: Lipopolysaccharide biosynthesis. | PFAM: Protein of unknown function DUF185; KEGG: pmf:P9303_15581 hypothetical protein. | 0.824 |
| EHA62420.1 | ndhH | Syn8016DRAFT_1715 | Syn8016DRAFT_1892 | Capsular exopolysaccharide family; TIGRFAM: Exopolysaccharide synthesis protein; KEGG: pmc:P9515_13861 hypothetical protein; PFAM: Lipopolysaccharide biosynthesis. | NAD(P)H-quinone oxidoreductase subunit H; 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. | 0.846 |