node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
STY0177 | STY0683 | gene:17584215 | gene:17584691 | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | 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. | 0.596 |
STY0177 | STY0686 | gene:17584215 | gene:17584693 | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 0.429 |
STY0177 | STY0780 | gene:17584215 | gene:17584786 | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | Dihydrolipoamide succinyltransferase component (E2); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). | 0.995 |
STY0177 | STY3209 | gene:17584215 | gene:17587084 | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | Glycine dehydrogenase (decarboxylating); 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. | 0.959 |
STY0177 | STY3210 | gene:17584215 | gene:17587085 | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | 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. | 0.972 |
STY0177 | lplA | gene:17584215 | gene:17588741 | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | Lipoate-protein ligase A; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. | 0.753 |
STY0404 | STY0683 | gene:17584432 | gene:17584691 | Delta-aminolevulinic acid dehydratase; Orthologue of E. coli hemB (HEM2_ECOLI); Fasta hit to HEM2_ECOLI (323 aa), 94% identity in 323 aa overlap; Belongs to the ALAD 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. | 0.598 |
STY0404 | STY2688 | gene:17584432 | gene:17586586 | Delta-aminolevulinic acid dehydratase; Orthologue of E. coli hemB (HEM2_ECOLI); Fasta hit to HEM2_ECOLI (323 aa), 94% identity in 323 aa overlap; Belongs to the ALAD family. | Coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. | 0.602 |
STY0683 | STY0177 | gene:17584691 | gene:17584215 | 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. | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | 0.596 |
STY0683 | STY0404 | gene:17584691 | gene:17584432 | 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. | Delta-aminolevulinic acid dehydratase; Orthologue of E. coli hemB (HEM2_ECOLI); Fasta hit to HEM2_ECOLI (323 aa), 94% identity in 323 aa overlap; Belongs to the ALAD family. | 0.598 |
STY0683 | STY0686 | gene:17584691 | gene:17584693 | 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. | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 0.999 |
STY0683 | STY0780 | gene:17584691 | gene:17584786 | 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. | Dihydrolipoamide succinyltransferase component (E2); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). | 0.611 |
STY0683 | STY2688 | gene:17584691 | gene:17586586 | 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. | Coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. | 0.608 |
STY0683 | STY3209 | gene:17584691 | gene:17587084 | 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. | Glycine dehydrogenase (decarboxylating); 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. | 0.648 |
STY0683 | STY3210 | gene:17584691 | gene:17587085 | 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. | 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. | 0.932 |
STY0683 | STY4817 | gene:17584691 | gene:17588639 | 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. | Probable inner membrane protein. Similar to Escherichia coli hypothetical protein YjgP SW:YJGP_ECOLI (P39340) (366 aa) fasta scores: E(): 0, 95.3% id in 359 aa and to Haemophilus influenzae hypothetical protein HI1704 SW:YJGP_HAEIN (P45333) (372 aa) fasta scores: E(): 0, 47.8% id in 358 aa. | 0.633 |
STY0683 | crcB | gene:17584691 | gene:17584688 | 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. | Putative membrane protein; Important for reducing fluoride concentration in the cell, thus reducing its toxicity; Belongs to the CrcB (TC 9.B.71) family. | 0.679 |
STY0683 | lplA | gene:17584691 | gene:17588741 | 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. | Lipoate-protein ligase A; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. | 0.980 |
STY0686 | STY0177 | gene:17584693 | gene:17584215 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Dihydrolipoamide dehydrogenase; Orthologue of E. coli lpdA (DLDH_ECOLI); Fasta hit to DLDH_ECOLI (473 aa), 98% identity in 473 aa overlap. | 0.429 |
STY0686 | STY0683 | gene:17584693 | gene:17584691 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 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. | 0.999 |