node1 | node2 | node1 annotation | node2 annotation | score |
A0A1X2H0T1 | A0A1X2H0U7 | BPL/LPL catalytic domain-containing protein. | BPL/LPL catalytic domain-containing protein. | 0.941 |
A0A1X2H0T1 | A0A1X2H2H6 | BPL/LPL catalytic domain-containing protein. | Dihydrolipoyl dehydrogenase. | 0.787 |
A0A1X2H0T1 | A0A1X2H870 | BPL/LPL catalytic domain-containing protein. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.865 |
A0A1X2H0T1 | A0A1X2HSI9 | BPL/LPL catalytic domain-containing protein. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.886 |
A0A1X2H0T1 | A0A1X2HWK2 | BPL/LPL catalytic domain-containing protein. | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | 0.960 |
A0A1X2H0U7 | A0A1X2H0T1 | BPL/LPL catalytic domain-containing protein. | BPL/LPL catalytic domain-containing protein. | 0.941 |
A0A1X2H0U7 | A0A1X2H2H6 | BPL/LPL catalytic domain-containing protein. | Dihydrolipoyl dehydrogenase. | 0.787 |
A0A1X2H0U7 | A0A1X2H870 | BPL/LPL catalytic domain-containing protein. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.865 |
A0A1X2H0U7 | A0A1X2HSI9 | BPL/LPL catalytic domain-containing protein. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.886 |
A0A1X2H0U7 | A0A1X2HWK2 | BPL/LPL catalytic domain-containing protein. | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | 0.960 |
A0A1X2H2H6 | A0A1X2H0T1 | Dihydrolipoyl dehydrogenase. | BPL/LPL catalytic domain-containing protein. | 0.787 |
A0A1X2H2H6 | A0A1X2H0U7 | Dihydrolipoyl dehydrogenase. | BPL/LPL catalytic domain-containing protein. | 0.787 |
A0A1X2H2H6 | A0A1X2HC65 | Dihydrolipoyl dehydrogenase. | Glycine cleavage system P protein; The glycine cleavage system catalyzes the degradation of glycine. | 0.885 |
A0A1X2H2H6 | A0A1X2HHL2 | Dihydrolipoyl dehydrogenase. | Serine hydroxymethyltransferase-domain-containing protein. | 0.809 |
A0A1X2H2H6 | A0A1X2HRM3 | Dihydrolipoyl dehydrogenase. | Aminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine; Belongs to the GcvT family. | 0.893 |
A0A1X2H2H6 | A0A1X2HSB1 | Dihydrolipoyl dehydrogenase. | FAD dependent oxidoreductase. | 0.733 |
A0A1X2H2H6 | A0A1X2HSI9 | Dihydrolipoyl dehydrogenase. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.508 |
A0A1X2H2H6 | A0A1X2HV21 | Dihydrolipoyl dehydrogenase. | DASH complex subunit Dad4-domain-containing protein. | 0.733 |
A0A1X2H2H6 | A0A1X2HWK2 | Dihydrolipoyl dehydrogenase. | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | 0.990 |
A0A1X2H870 | A0A1X2H0T1 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | BPL/LPL catalytic domain-containing protein. | 0.865 |