| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KWZ72155.1 | KWZ72156.1 | HMPREF3198_02253 | HMPREF3198_02254 | Acyltransferase; KEGG: bcv:Bcav_1904 3.9e-88 phospholipid/glycerol acyltransferase; K00655 1-acyl-sn-glycerol-3-phosphate acyltransferase; Psort location: Cytoplasmic, score: 7.50. | Hypothetical protein; Psort location: CytoplasmicMembrane, score: 9.55. | 0.555 |
| KWZ72155.1 | KWZ72157.1 | HMPREF3198_02253 | HMPREF3198_02255 | Acyltransferase; KEGG: bcv:Bcav_1904 3.9e-88 phospholipid/glycerol acyltransferase; K00655 1-acyl-sn-glycerol-3-phosphate acyltransferase; Psort location: Cytoplasmic, score: 7.50. | GIY-YIG catalytic domain protein; KEGG: bcv:Bcav_1900 1.8e-106 hypothetical protein; K02342 DNA polymerase III subunit epsilon; Psort location: Cytoplasmic, score: 9.67. | 0.605 |
| KWZ72155.1 | pfp | HMPREF3198_02253 | HMPREF3198_02252 | Acyltransferase; KEGG: bcv:Bcav_1904 3.9e-88 phospholipid/glycerol acyltransferase; K00655 1-acyl-sn-glycerol-3-phosphate acyltransferase; Psort location: Cytoplasmic, score: 7.50. | Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | 0.580 |
| KWZ72156.1 | KWZ72155.1 | HMPREF3198_02254 | HMPREF3198_02253 | Hypothetical protein; Psort location: CytoplasmicMembrane, score: 9.55. | Acyltransferase; KEGG: bcv:Bcav_1904 3.9e-88 phospholipid/glycerol acyltransferase; K00655 1-acyl-sn-glycerol-3-phosphate acyltransferase; Psort location: Cytoplasmic, score: 7.50. | 0.555 |
| KWZ72156.1 | KWZ72157.1 | HMPREF3198_02254 | HMPREF3198_02255 | Hypothetical protein; Psort location: CytoplasmicMembrane, score: 9.55. | GIY-YIG catalytic domain protein; KEGG: bcv:Bcav_1900 1.8e-106 hypothetical protein; K02342 DNA polymerase III subunit epsilon; Psort location: Cytoplasmic, score: 9.67. | 0.773 |
| KWZ72156.1 | pfp | HMPREF3198_02254 | HMPREF3198_02252 | Hypothetical protein; Psort location: CytoplasmicMembrane, score: 9.55. | Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | 0.402 |
| KWZ72157.1 | KWZ72155.1 | HMPREF3198_02255 | HMPREF3198_02253 | GIY-YIG catalytic domain protein; KEGG: bcv:Bcav_1900 1.8e-106 hypothetical protein; K02342 DNA polymerase III subunit epsilon; Psort location: Cytoplasmic, score: 9.67. | Acyltransferase; KEGG: bcv:Bcav_1904 3.9e-88 phospholipid/glycerol acyltransferase; K00655 1-acyl-sn-glycerol-3-phosphate acyltransferase; Psort location: Cytoplasmic, score: 7.50. | 0.605 |
| KWZ72157.1 | KWZ72156.1 | HMPREF3198_02255 | HMPREF3198_02254 | GIY-YIG catalytic domain protein; KEGG: bcv:Bcav_1900 1.8e-106 hypothetical protein; K02342 DNA polymerase III subunit epsilon; Psort location: Cytoplasmic, score: 9.67. | Hypothetical protein; Psort location: CytoplasmicMembrane, score: 9.55. | 0.773 |
| KWZ72157.1 | pfp | HMPREF3198_02255 | HMPREF3198_02252 | GIY-YIG catalytic domain protein; KEGG: bcv:Bcav_1900 1.8e-106 hypothetical protein; K02342 DNA polymerase III subunit epsilon; Psort location: Cytoplasmic, score: 9.67. | Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | 0.535 |
| pfp | KWZ72155.1 | HMPREF3198_02252 | HMPREF3198_02253 | Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | Acyltransferase; KEGG: bcv:Bcav_1904 3.9e-88 phospholipid/glycerol acyltransferase; K00655 1-acyl-sn-glycerol-3-phosphate acyltransferase; Psort location: Cytoplasmic, score: 7.50. | 0.580 |
| pfp | KWZ72156.1 | HMPREF3198_02252 | HMPREF3198_02254 | Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | Hypothetical protein; Psort location: CytoplasmicMembrane, score: 9.55. | 0.402 |
| pfp | KWZ72157.1 | HMPREF3198_02252 | HMPREF3198_02255 | Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | GIY-YIG catalytic domain protein; KEGG: bcv:Bcav_1900 1.8e-106 hypothetical protein; K02342 DNA polymerase III subunit epsilon; Psort location: Cytoplasmic, score: 9.67. | 0.535 |