| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaA | ilvA | HI_0286 | HI_0738.1 | Aminotransferase; Involved in the biosynthesis of alanine. | Threonine deaminase (ilvA); 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 (By similarity). | 0.537 |
| alaA | ilvD | HI_0286 | HI_0738 | Aminotransferase; Involved in the biosynthesis of alanine. | Dihydroxyacid dehydratase (ilvD); Similar to SP:P05791 GB:M10313 GB:K03503 GB:M32253 GB:X02413 percent identity: 76.87; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. | 0.929 |
| alaA | ilvE | HI_0286 | HI_1193 | Aminotransferase; Involved in the biosynthesis of alanine. | Branched-chain-amino-acid transaminase (ilvE); Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.936 |
| alaA | leuA | HI_0286 | HI_0986 | Aminotransferase; Involved in the biosynthesis of alanine. | 2-isopropylmalate synthase (leuA); Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.926 |
| alaA | metB | HI_0286 | HI_0086 | Aminotransferase; Involved in the biosynthesis of alanine. | Cystathionine gamma-synthase (metB); Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia (By similarity). | 0.505 |
| alaA | pflB | HI_0286 | HI_0180 | Aminotransferase; Involved in the biosynthesis of alanine. | Formate acetyltransferase (pfl); Similar to GB:X08035 SP:P09373 PID:42370 GB:U00096 PID:1651427 percent identity: 86.09; identified by sequence similarity; putative. | 0.921 |
| alaA | thrA | HI_0286 | HI_0089 | Aminotransferase; Involved in the biosynthesis of alanine. | Aspartokinase I / homoserine dehydrogenase I (thrA); Similar to SP:P00561 GB:M10644 GB:V00360 GB:V00361 PID:147979 percent identity: 62.21; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.930 |
| alaA | thrB | HI_0286 | HI_0088 | Aminotransferase; Involved in the biosynthesis of alanine. | Homoserine kinase (thrB); Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.526 |
| ilvA | alaA | HI_0738.1 | HI_0286 | Threonine deaminase (ilvA); 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 (By similarity). | Aminotransferase; Involved in the biosynthesis of alanine. | 0.537 |
| ilvA | ilvC | HI_0738.1 | HI_0682 | Threonine deaminase (ilvA); 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 (By similarity). | Ketol-acid reductoisomerase (ilvC); Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.631 |
| ilvA | ilvD | HI_0738.1 | HI_0738 | Threonine deaminase (ilvA); 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 (By similarity). | Dihydroxyacid dehydratase (ilvD); Similar to SP:P05791 GB:M10313 GB:K03503 GB:M32253 GB:X02413 percent identity: 76.87; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. | 0.967 |
| ilvA | ilvE | HI_0738.1 | HI_1193 | Threonine deaminase (ilvA); 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 (By similarity). | Branched-chain-amino-acid transaminase (ilvE); Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.984 |
| ilvA | ilvH | HI_0738.1 | HI_1584 | Threonine deaminase (ilvA); 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 (By similarity). | Acetolactate synthase III small subunit (ilvH); Similar to GB:D10483 SP:P00894 GB:X01609 PID:216495 PID:40846 percent identity: 65.62; identified by sequence similarity; putative; Belongs to the acetolactate synthase small subunit family. | 0.991 |
| ilvA | leuA | HI_0738.1 | HI_0986 | Threonine deaminase (ilvA); 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 (By similarity). | 2-isopropylmalate synthase (leuA); Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.678 |
| ilvA | metB | HI_0738.1 | HI_0086 | Threonine deaminase (ilvA); 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 (By similarity). | Cystathionine gamma-synthase (metB); Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia (By similarity). | 0.937 |
| ilvA | pflB | HI_0738.1 | HI_0180 | Threonine deaminase (ilvA); 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 (By similarity). | Formate acetyltransferase (pfl); Similar to GB:X08035 SP:P09373 PID:42370 GB:U00096 PID:1651427 percent identity: 86.09; identified by sequence similarity; putative. | 0.920 |
| ilvA | thrA | HI_0738.1 | HI_0089 | Threonine deaminase (ilvA); 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 (By similarity). | Aspartokinase I / homoserine dehydrogenase I (thrA); Similar to SP:P00561 GB:M10644 GB:V00360 GB:V00361 PID:147979 percent identity: 62.21; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.947 |
| ilvA | thrB | HI_0738.1 | HI_0088 | Threonine deaminase (ilvA); 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 (By similarity). | Homoserine kinase (thrB); Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.670 |
| ilvC | ilvA | HI_0682 | HI_0738.1 | Ketol-acid reductoisomerase (ilvC); Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Threonine deaminase (ilvA); 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 (By similarity). | 0.631 |
| ilvC | ilvD | HI_0682 | HI_0738 | Ketol-acid reductoisomerase (ilvC); Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Dihydroxyacid dehydratase (ilvD); Similar to SP:P05791 GB:M10313 GB:K03503 GB:M32253 GB:X02413 percent identity: 76.87; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. | 0.992 |
