| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hom | ilvA | azo2081 | azo0500 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Probable 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. | 0.781 |
| hom | ilvD | azo2081 | azo0632 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.498 |
| hom | ilvE1 | azo2081 | azo0133 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.676 |
| hom | pheA | azo2081 | azo1068 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity. | 0.739 |
| ilvA | hom | azo0500 | azo2081 | Probable 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 catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | 0.781 |
| ilvA | ilvD | azo0500 | azo0632 | Probable 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 fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.912 |
| ilvA | ilvE1 | azo0500 | azo0133 | Probable 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 transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.712 |
| ilvA | pheA | azo0500 | azo1068 | Probable 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. | Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity. | 0.605 |
| ilvA | putA | azo0500 | azo3753 | Probable 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 bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.404 |
| ilvD | hom | azo0632 | azo2081 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | 0.498 |
| ilvD | ilvA | azo0632 | azo0500 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Probable 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. | 0.912 |
| ilvD | ilvE1 | azo0632 | azo0133 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.958 |
| ilvD | leuA1 | azo0632 | azo3162 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate 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. | 0.982 |
| ilvD | leuA2 | azo0632 | azo3523 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate 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. | 0.987 |
| ilvD | mvaB | azo0632 | azo3065 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Hydroxymethylglutaryl-CoA lyase, MvaB. It catalyses the conversion of (S)-3-hydroxy-3-methylglutaryl-CoA to acetyl-CoA and acetoacetate during the final step of ketogenesis and leucine catabolism. Similar to trembl|Q8QGJ4 (60%) and to pir|H83394 (56%). InterPro (PF00682): HMG-CoA Lyase-like family; High confidence in function and specificity. | 0.776 |
| ilvD | nifV | azo0632 | azo0551 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Homocitrate synthase is involved in the biosynthesis of the iron-molybdenum cofactor of nitrogenase and catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate into homocitrate. Similar to sprot|NIFV_AZOVI (51%) and to sprot|NIV1_ANASP (42%). Pfam (PF00682): HMG-CoA Lyase-like family InterPro (PS00815): Alpha-isopropylmalate and homocitrate synthase; High confidence in function and specificity; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.811 |
| ilvD | panB | azo0632 | azo3144 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate 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. | 0.951 |
| ilvD | pheA | azo0632 | azo1068 | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid and 6-phosphogluconate dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity. | 0.627 |
| ilvE1 | hom | azo0133 | azo2081 | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | 0.676 |
| ilvE1 | ilvA | azo0133 | azo0500 | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Probable 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. | 0.712 |