| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMS39998.1 | AMS40951.1 | AA2016_1060 | AA2016_2021 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | 0.901 |
| AMS39998.1 | AMS43641.1 | AA2016_1060 | AA2016_4731 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | 0.937 |
| AMS39998.1 | AMS43649.1 | AA2016_1060 | AA2016_4739 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Hypothetical protein; Pfam:pfam00128 Alpha amylase, catalytic domain; Belongs to the glycosyl hydrolase 13 family. | 0.913 |
| AMS39998.1 | AMS43650.1 | AA2016_1060 | AA2016_4740 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | 0.923 |
| AMS39998.1 | AMS43654.1 | AA2016_1060 | AA2016_4744 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Glycogen phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | 0.917 |
| AMS39998.1 | glgC | AA2016_1060 | AA2016_4742 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family. | 0.917 |
| AMS40951.1 | AMS39998.1 | AA2016_2021 | AA2016_1060 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | 0.901 |
| AMS40951.1 | AMS43641.1 | AA2016_2021 | AA2016_4731 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | 0.939 |
| AMS40951.1 | AMS43649.1 | AA2016_2021 | AA2016_4739 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Hypothetical protein; Pfam:pfam00128 Alpha amylase, catalytic domain; Belongs to the glycosyl hydrolase 13 family. | 0.913 |
| AMS40951.1 | AMS43650.1 | AA2016_2021 | AA2016_4740 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | 0.923 |
| AMS40951.1 | AMS43654.1 | AA2016_2021 | AA2016_4744 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Glycogen phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | 0.917 |
| AMS40951.1 | glgC | AA2016_2021 | AA2016_4742 | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family. | 0.917 |
| AMS41536.1 | AMS43650.1 | AA2016_2611 | AA2016_4740 | Hypothetical protein. | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | 0.723 |
| AMS41536.1 | AMS43654.1 | AA2016_2611 | AA2016_4744 | Hypothetical protein. | Glycogen phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | 0.897 |
| AMS41536.1 | glgB | AA2016_2611 | AA2016_4743 | Hypothetical protein. | Glycogen branching protein; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position; Belongs to the glycosyl hydrolase 13 family. GlgB subfamily. | 0.772 |
| AMS43641.1 | AMS39998.1 | AA2016_4731 | AA2016_1060 | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | 0.937 |
| AMS43641.1 | AMS40951.1 | AA2016_4731 | AA2016_2021 | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | UTP--glucose-1-phosphate uridylyltransferase; Pfam:pfam00483 Nucleotidyl transferase. | 0.939 |
| AMS43641.1 | AMS43649.1 | AA2016_4731 | AA2016_4739 | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | Hypothetical protein; Pfam:pfam00128 Alpha amylase, catalytic domain; Belongs to the glycosyl hydrolase 13 family. | 0.917 |
| AMS43641.1 | AMS43650.1 | AA2016_4731 | AA2016_4740 | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | 0.943 |
| AMS43641.1 | AMS43654.1 | AA2016_4731 | AA2016_4744 | Pfam:pfam02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I. | Glycogen phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | 0.931 |