| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Neut_0865 | Neut_0866 | Neut_0865 | Neut_0866 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | 0.750 |
| Neut_0865 | ilvA | Neut_0865 | Neut_1160 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | L-threonine ammonia-lyase; 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. | 0.537 |
| Neut_0865 | ilvD | Neut_0865 | Neut_2238 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | KEGG: neu:NE0104 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.420 |
| Neut_0865 | ilvE | Neut_0865 | Neut_2005 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | Branched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.871 |
| Neut_0865 | leuA | Neut_0865 | Neut_1244 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | 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. | 0.471 |
| Neut_0865 | thrB | Neut_0865 | Neut_0775 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | Homoserine kinase; KEGG: neu:NE1471 putative homoserine kinase protein; TIGRFAM: homoserine kinase; PFAM: aminoglycoside phosphotransferase; Belongs to the pseudomonas-type ThrB family. | 0.928 |
| Neut_0866 | Neut_0865 | Neut_0866 | Neut_0865 | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | 0.750 |
| Neut_0866 | ilvD | Neut_0866 | Neut_2238 | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | KEGG: neu:NE0104 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.917 |
| Neut_0866 | ilvE | Neut_0866 | Neut_2005 | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | Branched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.910 |
| Neut_0866 | leuA | Neut_0866 | Neut_1244 | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | 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. | 0.910 |
| Neut_0866 | nadE | Neut_0866 | Neut_2008 | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.494 |
| Neut_0954 | ilvE | Neut_0954 | Neut_2005 | TIGRFAM: glutamate--cysteine ligase; KEGG: neu:NE1294 putative glutamate--cysteine ligase. | Branched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.900 |
| Neut_2006 | ilvE | Neut_2006 | Neut_2005 | KEGG: neu:NE1894 hypothetical protein. | Branched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.795 |
| Neut_2006 | nadE | Neut_2006 | Neut_2008 | KEGG: neu:NE1894 hypothetical protein. | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.581 |
| ilvA | Neut_0865 | Neut_1160 | Neut_0865 | L-threonine ammonia-lyase; 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. | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | 0.537 |
| ilvA | ilvD | Neut_1160 | Neut_2238 | L-threonine ammonia-lyase; 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. | KEGG: neu:NE0104 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.895 |
| ilvA | ilvE | Neut_1160 | Neut_2005 | L-threonine ammonia-lyase; 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 apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.913 |
| ilvA | leuA | Neut_1160 | Neut_1244 | L-threonine ammonia-lyase; 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 1 subfamily. | 0.441 |
| ilvD | Neut_0865 | Neut_2238 | Neut_0865 | KEGG: neu:NE0104 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: neu:NE2369 homoserine dehydrogenase. | 0.420 |
| ilvD | Neut_0866 | Neut_2238 | Neut_0866 | KEGG: neu:NE0104 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | PFAM: aminotransferase, class I and II; KEGG: neu:NE2368 aspartate aminotransferase. | 0.917 |