node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
catE | rtbJ | BSU08240 | BSU19230 | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. | 0.768 |
catE | ydfN | BSU08240 | BSU05480 | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | 0.751 |
catE | ykvN | BSU08240 | BSU13760 | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.499 |
catE | yodC | BSU08240 | BSU19550 | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | 0.855 |
ndoA | ykvN | BSU04660 | BSU13760 | Endoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U. Yields cleavage products with 3' phosphate and 5' hydroxyl groups. Cannot digest substrate with a UUdUACAUAA cleavage site. Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.457 |
rtbJ | catE | BSU19230 | BSU08240 | Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | 0.768 |
rtbJ | ydfN | BSU19230 | BSU05480 | Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | 0.842 |
rtbJ | ykvN | BSU19230 | BSU13760 | Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.453 |
rtbJ | yodC | BSU19230 | BSU19550 | Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | 0.919 |
ydeQ | ydfN | BSU05300 | BSU05480 | Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family. | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | 0.598 |
ydeQ | ykvN | BSU05300 | BSU13760 | Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.685 |
ydeQ | yodC | BSU05300 | BSU19550 | Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family. | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | 0.514 |
ydeQ | yqiG | BSU05300 | BSU24210 | Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family. | Putative NADH-dependent flavin oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. | 0.697 |
ydfN | catE | BSU05480 | BSU08240 | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | 0.751 |
ydfN | rtbJ | BSU05480 | BSU19230 | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. | 0.842 |
ydfN | ydeQ | BSU05480 | BSU05300 | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family. | 0.598 |
ydfN | ykvN | BSU05480 | BSU13760 | Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.682 |
yhxC | ykvN | BSU10400 | BSU13760 | Putative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.688 |
ykvN | catE | BSU13760 | BSU08240 | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. | 0.499 |
ykvN | ndoA | BSU13760 | BSU04660 | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | Endoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U. Yields cleavage products with 3' phosphate and 5' hydroxyl groups. Cannot digest substrate with a UUdUACAUAA cleavage site. Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter. | 0.457 |