| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| groEL | trxA | BSU06030 | BSU28500 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.891 |
| groEL | trxB | BSU06030 | BSU34790 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.500 |
| groEL | ydfQ | BSU06030 | BSU05510 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.688 |
| groEL | yosR | BSU06030 | BSU20030 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | SPbeta phage putative thiol disulfide oxidoreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the thioredoxin family. | 0.688 |
| groEL | ytpP | BSU06030 | BSU29840 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.688 |
| groEL | yusE | BSU06030 | BSU32770 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.445 |
| trxA | groEL | BSU28500 | BSU06030 | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.891 |
| trxA | trxB | BSU28500 | BSU34790 | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.999 |
| trxA | yneN | BSU28500 | BSU18010 | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Putative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family. | 0.656 |
| trxA | ytpP | BSU28500 | BSU29840 | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.656 |
| trxA | yusE | BSU28500 | BSU32770 | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.502 |
| trxB | groEL | BSU34790 | BSU06030 | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.500 |
| trxB | trxA | BSU34790 | BSU28500 | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.999 |
| trxB | ydfQ | BSU34790 | BSU05510 | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.422 |
| trxB | yosR | BSU34790 | BSU20030 | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | SPbeta phage putative thiol disulfide oxidoreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the thioredoxin family. | 0.646 |
| trxB | ytpP | BSU34790 | BSU29840 | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.693 |
| trxB | yusE | BSU34790 | BSU32770 | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.486 |
| ydfQ | groEL | BSU05510 | BSU06030 | Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.688 |
| ydfQ | trxB | BSU05510 | BSU34790 | Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.422 |
| ydfQ | yneN | BSU05510 | BSU18010 | Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family. | 0.787 |