| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKJ43500.1 | AKJ43881.1 | QQ39_16755 | QQ39_12130 | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.449 |
| AKJ43500.1 | ilvA | QQ39_16755 | QQ39_17790 | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.818 |
| AKJ43500.1 | ilvE | QQ39_16755 | QQ39_17800 | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.912 |
| AKJ43500.1 | metL | QQ39_16755 | QQ39_16750 | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
| AKJ43500.1 | thrA | QQ39_16755 | QQ39_03920 | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.936 |
| AKJ43881.1 | AKJ43500.1 | QQ39_12130 | QQ39_16755 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.449 |
| AKJ43881.1 | avtA | QQ39_12130 | QQ39_00605 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Valine--pyruvate aminotransferase; Transaminase C; catalyzes transamination of alanine, valine, and 2-aminobutyrate with their respective 2-keto acids; also catalyzes terminal step in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.905 |
| AKJ43881.1 | ilvD | QQ39_12130 | QQ39_17795 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.920 |
| AKJ43881.1 | ilvE | QQ39_12130 | QQ39_17800 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.919 |
| AKJ43881.1 | leuA | QQ39_12130 | QQ39_04405 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2-isopropylmalate synthase; 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. | 0.919 |
| AKJ43881.1 | metL | QQ39_12130 | QQ39_16750 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.650 |
| AKJ43881.1 | thrA | QQ39_12130 | QQ39_03920 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.650 |
| avtA | AKJ43881.1 | QQ39_00605 | QQ39_12130 | Valine--pyruvate aminotransferase; Transaminase C; catalyzes transamination of alanine, valine, and 2-aminobutyrate with their respective 2-keto acids; also catalyzes terminal step in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.905 |
| avtA | ilvD | QQ39_00605 | QQ39_17795 | Valine--pyruvate aminotransferase; Transaminase C; catalyzes transamination of alanine, valine, and 2-aminobutyrate with their respective 2-keto acids; also catalyzes terminal step in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.908 |
| avtA | ilvE | QQ39_00605 | QQ39_17800 | Valine--pyruvate aminotransferase; Transaminase C; catalyzes transamination of alanine, valine, and 2-aminobutyrate with their respective 2-keto acids; also catalyzes terminal step in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.914 |
| avtA | leuA | QQ39_00605 | QQ39_04405 | Valine--pyruvate aminotransferase; Transaminase C; catalyzes transamination of alanine, valine, and 2-aminobutyrate with their respective 2-keto acids; also catalyzes terminal step in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2-isopropylmalate synthase; 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. | 0.902 |
| ilvA | AKJ43500.1 | QQ39_17790 | QQ39_16755 | 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. | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.818 |
| ilvA | ilvD | QQ39_17790 | QQ39_17795 | 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. | Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.951 |
| ilvA | ilvE | QQ39_17790 | QQ39_17800 | 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.940 |
| ilvA | ilvM | QQ39_17790 | QQ39_17805 | 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. | Acetolactate synthase 2 regulatory subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.959 |