| 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 | ilvE2 | azo2081 | azo2775 | 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. | 0.953 |
| 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 |
| hom | thrB | azo2081 | azo3604 | 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 homoserine kinase. Homology to thrB of M. flagellum of 51% (sprot|KHSE_METFL). CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-homoserine. Pfam: Aminoglycoside phosphotransferase no signal peptide no TMHs; High confidence in function and specificity; Belongs to the pseudomonas-type ThrB family. | 0.958 |
| hom | thrH | azo2081 | azo3743 | 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 homoserine kinase; ThrH encodes a protein with an in vivo homoserine-kinase-like activity in P. aeruginosa. Homoserine kinase,the product of the thrB gene, catalyzes an obligatory step of threonine biosynthesis. Similar trembl|Q9I2Y2 (62%). Pfam (PF00702): haloacid dehalogenase-like hydrolase; Function unclear. | 0.913 |
| hom | yfbQ | azo2081 | azo2082 | 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. | Aspartate aminotransferase is important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. The enzyme catalyses the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate Similar to trembl|Q8XZR9 (72%),to trembl|Q9RAN0 (62%) and to sprot|YFBQ_ECOLI (57%). Pfam (PF00155): Aminotransferases class-I; Specificity unclear. | 0.842 |
| 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 | ilvE2 | azo0500 | azo2775 | 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. | 0.940 |
| 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 | thrH | azo0500 | azo3743 | 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 homoserine kinase; ThrH encodes a protein with an in vivo homoserine-kinase-like activity in P. aeruginosa. Homoserine kinase,the product of the thrB gene, catalyzes an obligatory step of threonine biosynthesis. Similar trembl|Q9I2Y2 (62%). Pfam (PF00702): haloacid dehalogenase-like hydrolase; Function unclear. | 0.901 |
| ilvA | yfbQ | azo0500 | azo2082 | 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. | Aspartate aminotransferase is important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. The enzyme catalyses the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate Similar to trembl|Q8XZR9 (72%),to trembl|Q9RAN0 (62%) and to sprot|YFBQ_ECOLI (57%). Pfam (PF00155): Aminotransferases class-I; Specificity unclear. | 0.415 |
| 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 | ilvE2 | azo0632 | azo2775 | 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. | 0.991 |
| 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 | 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 |