| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CV_4309 | ilvA | CV_4309 | CV_3093 | Probable L-allo-threonine aldolase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG2008. | Threonine dehydratase; 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. | 0.923 |
| CV_4309 | tdcB | CV_4309 | CV_3250 | Probable L-allo-threonine aldolase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG2008. | Threonine dehydratase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1171. | 0.923 |
| CV_4309 | tdh | CV_4309 | CV_1651 | Probable L-allo-threonine aldolase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG2008. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.906 |
| CV_4309 | thrC | CV_4309 | CV_0997 | Probable L-allo-threonine aldolase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG2008. | Threonine synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0498. | 0.934 |
| ilvA | CV_4309 | CV_3093 | CV_4309 | Threonine dehydratase; 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. | Probable L-allo-threonine aldolase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG2008. | 0.923 |
| ilvA | leuD1 | CV_3093 | CV_2168 | Threonine dehydratase; 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. | 0.413 |
| ilvA | lysC | CV_3093 | CV_1018 | Threonine dehydratase; 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. | Aspartate kinase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0527; Belongs to the aspartokinase family. | 0.498 |
| ilvA | metL | CV_3093 | CV_0996 | Threonine dehydratase; 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 dehydrogenase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0460. | 0.508 |
| ilvA | tdcB | CV_3093 | CV_3250 | Threonine dehydratase; 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. | Threonine dehydratase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1171. | 0.915 |
| ilvA | tdh | CV_3093 | CV_1651 | Threonine dehydratase; 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 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| ilvA | thrC | CV_3093 | CV_0997 | Threonine dehydratase; 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. | Threonine synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0498. | 0.957 |
| leuD1 | ilvA | CV_2168 | CV_3093 | 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. | Threonine dehydratase; 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. | 0.413 |
| leuD1 | metL | CV_2168 | CV_0996 | 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. | Homoserine dehydrogenase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0460. | 0.423 |
| leuD1 | tdcB | CV_2168 | CV_3250 | 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. | Threonine dehydratase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1171. | 0.407 |
| leuD1 | thrC | CV_2168 | CV_0997 | 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. | Threonine synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0498. | 0.851 |
| lysC | ilvA | CV_1018 | CV_3093 | Aspartate kinase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0527; Belongs to the aspartokinase family. | Threonine dehydratase; 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. | 0.498 |
| lysC | metL | CV_1018 | CV_0996 | Aspartate kinase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0527; Belongs to the aspartokinase family. | Homoserine dehydrogenase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0460. | 0.986 |
| lysC | serC | CV_1018 | CV_2301 | Aspartate kinase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0527; Belongs to the aspartokinase family. | Phosphoserine transaminase; 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. | 0.547 |
| lysC | tdcB | CV_1018 | CV_3250 | Aspartate kinase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0527; Belongs to the aspartokinase family. | Threonine dehydratase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1171. | 0.498 |
| lysC | thrC | CV_1018 | CV_0997 | Aspartate kinase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0527; Belongs to the aspartokinase family. | Threonine synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0498. | 0.905 |