| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KML36105.1 | fabG | VL14_21830 | VL14_03435 | Glucose-1-phosphate cytidylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.544 |
| KML36105.1 | secY | VL14_21830 | VL14_20205 | Glucose-1-phosphate cytidylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.408 |
| KML39828.1 | fabG | VL14_14960 | VL14_03435 | Sodium:proton exchanger; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.544 |
| KML45275.1 | fabG | VL14_03440 | VL14_03435 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.530 |
| KML46629.1 | fabG | VL14_00620 | VL14_03435 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.404 |
| KML46629.1 | secY | VL14_00620 | VL14_20205 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.570 |
| fabG | KML36105.1 | VL14_03435 | VL14_21830 | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Glucose-1-phosphate cytidylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.544 |
| fabG | KML39828.1 | VL14_03435 | VL14_14960 | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Sodium:proton exchanger; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.544 |
| fabG | KML45275.1 | VL14_03435 | VL14_03440 | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.530 |
| fabG | KML46629.1 | VL14_03435 | VL14_00620 | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.404 |
| fabG | secY | VL14_03435 | VL14_20205 | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.416 |
| secY | KML36105.1 | VL14_20205 | VL14_21830 | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Glucose-1-phosphate cytidylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.408 |
| secY | KML46629.1 | VL14_20205 | VL14_00620 | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.570 |
| secY | fabG | VL14_20205 | VL14_03435 | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.416 |
