| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABO_1183 | ilvD-1 | ABO_1183 | ABO_0180 | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.907 |
| ABO_1183 | ilvD2 | ABO_1183 | ABO_2312 | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | Dihydroxy-acid dehydratase; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.907 |
| ABO_1183 | ilvE | ABO_1183 | ABO_2301 | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.906 |
| ABO_1183 | leuA | ABO_1183 | ABO_0638 | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | 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. | 0.903 |
| ABO_1183 | leuA-2 | ABO_1183 | ABO_2437 | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | 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 2 subfamily. | 0.903 |
| gshA | ilvE | ABO_0263 | ABO_2301 | (glutamate-cysteine ligase) identified by sequence similarity; putative; High confidence in function and specificity; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.900 |
| hom | ilvE | ABO_0806 | ABO_2301 | Homoserine dehydrogenase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00742 InterPro: Homoserine dehydrogenase; High confidence in function and specificity. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.851 |
| ilvA | ilvD-1 | ABO_2605 | ABO_0180 | Threonine dehydratase, biosynthetic; 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; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.759 |
| ilvA | ilvD2 | ABO_2605 | ABO_2312 | Threonine dehydratase, biosynthetic; 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; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.870 |
| ilvA | ilvE | ABO_2605 | ABO_2301 | Threonine dehydratase, biosynthetic; 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. | 0.934 |
| ilvA | leuA-2 | ABO_2605 | ABO_2437 | Threonine dehydratase, biosynthetic; 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. | 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 2 subfamily. | 0.404 |
| ilvD-1 | ABO_1183 | ABO_0180 | ABO_1183 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | 0.907 |
| ilvD-1 | ilvA | ABO_0180 | ABO_2605 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Threonine dehydratase, biosynthetic; 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. | 0.759 |
| ilvD-1 | ilvD2 | ABO_0180 | ABO_2312 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.905 |
| ilvD-1 | ilvE | ABO_0180 | ABO_2301 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.962 |
| ilvD-1 | leuA | ABO_0180 | ABO_0638 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 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. | 0.960 |
| ilvD-1 | leuA-2 | ABO_0180 | ABO_2437 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 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 2 subfamily. | 0.930 |
| ilvD-1 | panB | ABO_0180 | ABO_0337 | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. | 0.919 |
| ilvD2 | ABO_1183 | ABO_2312 | ABO_1183 | Dihydroxy-acid dehydratase; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | (aminotransferase, putative) identified by match to PFAM protein family HMMPF00155; putative InterPro: Aminotransferases class-I; Family membership. | 0.907 |
| ilvD2 | ilvA | ABO_2312 | ABO_2605 | Dihydroxy-acid dehydratase; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Threonine dehydratase, biosynthetic; 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. | 0.870 |