| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Krad_1228 | Krad_3279 | Krad_1228 | Krad_3279 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | 0.997 |
| Krad_1228 | Krad_4031 | Krad_1228 | Krad_4031 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | PFAM: biotin/lipoate A/B protein ligase; KEGG: sco:SCO6423 putative lipoate-protein ligase. | 0.921 |
| Krad_1228 | acpP | Krad_1228 | Krad_3345 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | Phosphopantetheine-binding; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 0.532 |
| Krad_1228 | gcvH | Krad_1228 | Krad_3097 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | 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. | 0.934 |
| Krad_1228 | gcvP | Krad_1228 | Krad_3090 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.981 |
| Krad_1228 | lipA | Krad_1228 | Krad_3288 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | 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. | 0.679 |
| Krad_1228 | lipB | Krad_1228 | Krad_3284 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | Lipoate-protein ligase B; 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. | 0.607 |
| Krad_3279 | Krad_1228 | Krad_3279 | Krad_1228 | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | 0.997 |
| Krad_3279 | Krad_4031 | Krad_3279 | Krad_4031 | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | PFAM: biotin/lipoate A/B protein ligase; KEGG: sco:SCO6423 putative lipoate-protein ligase. | 0.720 |
| Krad_3279 | gcvH | Krad_3279 | Krad_3097 | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | 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. | 0.674 |
| Krad_3279 | gcvP | Krad_3279 | Krad_3090 | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.597 |
| Krad_3279 | lipA | Krad_3279 | Krad_3288 | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | 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. | 0.683 |
| Krad_3279 | lipB | Krad_3279 | Krad_3284 | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | Lipoate-protein ligase B; 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. | 0.684 |
| Krad_3283 | lipB | Krad_3283 | Krad_3284 | PFAM: peptidase S51 dipeptidase E; KEGG: art:Arth_0136 peptidase S51, dipeptidase E; Belongs to the peptidase S51 family. | Lipoate-protein ligase B; 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. | 0.777 |
| Krad_3346 | acpP | Krad_3346 | Krad_3345 | Beta-ketoacyl synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Phosphopantetheine-binding; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 0.996 |
| Krad_3346 | lipB | Krad_3346 | Krad_3284 | Beta-ketoacyl synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate-protein ligase B; 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. | 0.823 |
| Krad_4031 | Krad_1228 | Krad_4031 | Krad_1228 | PFAM: biotin/lipoate A/B protein ligase; KEGG: sco:SCO6423 putative lipoate-protein ligase. | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: art:Arth_2645 2-oxoglutarate dehydrogenase, E1 subunit. | 0.921 |
| Krad_4031 | Krad_3279 | Krad_4031 | Krad_3279 | PFAM: biotin/lipoate A/B protein ligase; KEGG: sco:SCO6423 putative lipoate-protein ligase. | TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: aau:AAur_1755 putative 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. | 0.720 |
| Krad_4031 | gcvH | Krad_4031 | Krad_3097 | PFAM: biotin/lipoate A/B protein ligase; KEGG: sco:SCO6423 putative lipoate-protein ligase. | 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. | 0.955 |
| Krad_4031 | lipA | Krad_4031 | Krad_3288 | PFAM: biotin/lipoate A/B protein ligase; KEGG: sco:SCO6423 putative lipoate-protein ligase. | 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. | 0.945 |