node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDN49807.1 | lipA | SAMN04488516_102312 | SAMN04488516_10520 | Phosphoribosyl 1,2-cyclic phosphodiesterase. | Lipoic acid synthetase; 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. | 0.593 |
SDN69486.1 | lipA | SAMN04488516_10518 | SAMN04488516_10520 | Aspartate/methionine/tyrosine aminotransferase. | Lipoic acid synthetase; 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. | 0.516 |
SDN69486.1 | lipB | SAMN04488516_10518 | SAMN04488516_10519 | Aspartate/methionine/tyrosine aminotransferase. | Lipoyl(octanoyl) transferase; 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. | 0.508 |
SDN69486.1 | nadE | SAMN04488516_10518 | SAMN04488516_11044 | Aspartate/methionine/tyrosine aminotransferase. | NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.640 |
SDN69567.1 | lipA | SAMN04488516_10521 | SAMN04488516_10520 | PD-(D/E)XK nuclease superfamily protein. | Lipoic acid synthetase; 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. | 0.538 |
SDN69567.1 | lipB | SAMN04488516_10521 | SAMN04488516_10519 | PD-(D/E)XK nuclease superfamily protein. | Lipoyl(octanoyl) transferase; 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. | 0.538 |
SDN75185.1 | lipA | SAMN04488516_10656 | SAMN04488516_10520 | Hypothetical protein. | Lipoic acid synthetase; 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. | 0.547 |
SDN78845.1 | SDN79663.1 | SAMN04488516_10724 | SAMN04488516_10748 | 8-oxo-dGTP diphosphatase; Belongs to the Nudix hydrolase family. | Transketolase; Belongs to the transketolase family. | 0.581 |
SDN78845.1 | SDN96243.1 | SAMN04488516_10724 | SAMN04488516_11335 | 8-oxo-dGTP diphosphatase; Belongs to the Nudix hydrolase family. | Dihydrolipoamide dehydrogenase. | 0.553 |
SDN78845.1 | lipA | SAMN04488516_10724 | SAMN04488516_10520 | 8-oxo-dGTP diphosphatase; Belongs to the Nudix hydrolase family. | Lipoic acid synthetase; 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. | 0.554 |
SDN78845.1 | nadE | SAMN04488516_10724 | SAMN04488516_11044 | 8-oxo-dGTP diphosphatase; Belongs to the Nudix hydrolase family. | NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.936 |
SDN79663.1 | SDN78845.1 | SAMN04488516_10748 | SAMN04488516_10724 | Transketolase; Belongs to the transketolase family. | 8-oxo-dGTP diphosphatase; Belongs to the Nudix hydrolase family. | 0.581 |
SDN79663.1 | SDN96243.1 | SAMN04488516_10748 | SAMN04488516_11335 | Transketolase; Belongs to the transketolase family. | Dihydrolipoamide dehydrogenase. | 0.778 |
SDN79663.1 | lipA | SAMN04488516_10748 | SAMN04488516_10520 | Transketolase; Belongs to the transketolase family. | Lipoic acid synthetase; 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. | 0.517 |
SDN79663.1 | nadE | SAMN04488516_10748 | SAMN04488516_11044 | Transketolase; Belongs to the transketolase family. | NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.583 |
SDN96243.1 | SDN78845.1 | SAMN04488516_11335 | SAMN04488516_10724 | Dihydrolipoamide dehydrogenase. | 8-oxo-dGTP diphosphatase; Belongs to the Nudix hydrolase family. | 0.553 |
SDN96243.1 | SDN79663.1 | SAMN04488516_11335 | SAMN04488516_10748 | Dihydrolipoamide dehydrogenase. | Transketolase; Belongs to the transketolase family. | 0.778 |
SDN96243.1 | gcvH | SAMN04488516_11335 | SAMN04488516_11332 | Dihydrolipoamide dehydrogenase. | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.985 |
SDN96243.1 | lipA | SAMN04488516_11335 | SAMN04488516_10520 | Dihydrolipoamide dehydrogenase. | Lipoic acid synthetase; 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. | 0.718 |
SDN96243.1 | lipB | SAMN04488516_11335 | SAMN04488516_10519 | Dihydrolipoamide dehydrogenase. | Lipoyl(octanoyl) transferase; 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. | 0.435 |