| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACWI_25950 | tdcB | ACWI_25950 | ACWI_26770 | YheO-like PAS domain protein. | L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.416 |
| ACWI_25950 | tdcF | ACWI_25950 | ACWI_25940 | YheO-like PAS domain protein. | Putative reactive intermediate deaminase TdcF. | 0.632 |
| fusA_1 | pksJ | ACWI_25830 | ACWI_26840 | Elongation factor G. | Polyketide synthase PksJ. | 0.711 |
| fusA_1 | tdcF | ACWI_25830 | ACWI_25940 | Elongation factor G. | Putative reactive intermediate deaminase TdcF. | 0.569 |
| glxK | tdcF | ACWI_35230 | ACWI_25940 | Glycerate kinase; Belongs to the glycerate kinase type-1 family. | Putative reactive intermediate deaminase TdcF. | 0.620 |
| pksJ | fusA_1 | ACWI_26840 | ACWI_25830 | Polyketide synthase PksJ. | Elongation factor G. | 0.711 |
| pksJ | rluD_1 | ACWI_26840 | ACWI_18720 | Polyketide synthase PksJ. | Ribosomal large subunit pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.752 |
| pksJ | tdcB | ACWI_26840 | ACWI_26770 | Polyketide synthase PksJ. | L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.729 |
| pksJ | tdcF | ACWI_26840 | ACWI_25940 | Polyketide synthase PksJ. | Putative reactive intermediate deaminase TdcF. | 0.596 |
| pksJ | tpiA_1 | ACWI_26840 | ACWI_08100 | Polyketide synthase PksJ. | Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. | 0.503 |
| pksJ | tpiA_2 | ACWI_26840 | ACWI_34100 | Polyketide synthase PksJ. | Triosephosphate isomerase. | 0.503 |
| pksJ | tyrB | ACWI_26840 | ACWI_12030 | Polyketide synthase PksJ. | Aromatic-amino-acid aminotransferase. | 0.791 |
| rluD_1 | pksJ | ACWI_18720 | ACWI_26840 | Ribosomal large subunit pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Polyketide synthase PksJ. | 0.752 |
| rluD_1 | tdcF | ACWI_18720 | ACWI_25940 | Ribosomal large subunit pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Putative reactive intermediate deaminase TdcF. | 0.605 |
| rluD_1 | tpiA_1 | ACWI_18720 | ACWI_08100 | Ribosomal large subunit pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. | 0.490 |
| rluD_1 | tpiA_2 | ACWI_18720 | ACWI_34100 | Ribosomal large subunit pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Triosephosphate isomerase. | 0.551 |
| rph | tdcF | ACWI_22680 | ACWI_25940 | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | Putative reactive intermediate deaminase TdcF. | 0.684 |
| tdcB | ACWI_25950 | ACWI_26770 | ACWI_25950 | L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | YheO-like PAS domain protein. | 0.416 |
| tdcB | pksJ | ACWI_26770 | ACWI_26840 | L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Polyketide synthase PksJ. | 0.729 |
| tdcB | tdcF | ACWI_26770 | ACWI_25940 | L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Putative reactive intermediate deaminase TdcF. | 0.732 |