| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJI78096.1 | ilvA | CSING_02730 | CSING_08880 | L-threonine aldolase; PFAM: Beta-eliminating lyase. | L-threonine ammonia-lyase; 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. | 0.915 |
| AJI78096.1 | thrC | CSING_02730 | CSING_09490 | L-threonine aldolase; PFAM: Beta-eliminating lyase. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.928 |
| AJI79413.1 | AJI79414.1 | CSING_09475 | CSING_09480 | ADP-ribose pyrophosphatase; PFAM: NUDIX domain. | PFAM: Trypsin. | 0.796 |
| AJI79413.1 | AJI79417.1 | CSING_09475 | CSING_09495 | ADP-ribose pyrophosphatase; PFAM: NUDIX domain. | Sugar phosphate permease; PFAM: Major Facilitator Superfamily. | 0.564 |
| AJI79413.1 | thrC | CSING_09475 | CSING_09490 | ADP-ribose pyrophosphatase; PFAM: NUDIX domain. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.634 |
| AJI79414.1 | AJI79413.1 | CSING_09480 | CSING_09475 | PFAM: Trypsin. | ADP-ribose pyrophosphatase; PFAM: NUDIX domain. | 0.796 |
| AJI79414.1 | AJI79417.1 | CSING_09480 | CSING_09495 | PFAM: Trypsin. | Sugar phosphate permease; PFAM: Major Facilitator Superfamily. | 0.574 |
| AJI79414.1 | thrC | CSING_09480 | CSING_09490 | PFAM: Trypsin. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.649 |
| AJI79417.1 | AJI79413.1 | CSING_09495 | CSING_09475 | Sugar phosphate permease; PFAM: Major Facilitator Superfamily. | ADP-ribose pyrophosphatase; PFAM: NUDIX domain. | 0.564 |
| AJI79417.1 | AJI79414.1 | CSING_09495 | CSING_09480 | Sugar phosphate permease; PFAM: Major Facilitator Superfamily. | PFAM: Trypsin. | 0.574 |
| AJI79417.1 | thrC | CSING_09495 | CSING_09490 | Sugar phosphate permease; PFAM: Major Facilitator Superfamily. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.687 |
| hom | ilvA | CSING_05735 | CSING_08880 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | L-threonine ammonia-lyase; 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. | 0.847 |
| hom | lysC | CSING_05735 | CSING_01005 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Aspartate kinase; PFAM: ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; Belongs to the aspartokinase family. | 0.985 |
| hom | serC | CSING_05735 | CSING_04315 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Phosphoserine aminotransferase apoenzyme; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.401 |
| hom | thrB | CSING_05735 | CSING_05740 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.999 |
| hom | thrC | CSING_05735 | CSING_09490 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.973 |
| ilvA | AJI78096.1 | CSING_08880 | CSING_02730 | L-threonine ammonia-lyase; 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. | L-threonine aldolase; PFAM: Beta-eliminating lyase. | 0.915 |
| ilvA | hom | CSING_08880 | CSING_05735 | L-threonine ammonia-lyase; 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. | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | 0.847 |
| ilvA | leuD | CSING_08880 | CSING_06420 | L-threonine ammonia-lyase; 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. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.604 |
| ilvA | thrB | CSING_08880 | CSING_05740 | L-threonine ammonia-lyase; 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.826 |