node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACX95368.1 | ilvE | Hneap_0513 | Hneap_2135 | TIGRFAM: glutamate/cysteine ligase; PFAM: glutamate--cysteine ligase GshA; KEGG: tbd:Tbd_2408 glutamate--cysteine ligase GshA. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.900 |
ACX95368.1 | thrB | Hneap_0513 | Hneap_1690 | TIGRFAM: glutamate/cysteine ligase; PFAM: glutamate--cysteine ligase GshA; KEGG: tbd:Tbd_2408 glutamate--cysteine ligase GshA. | KEGG: tcx:Tcr_0043 homoserine kinase; TIGRFAM: homoserine kinase; PFAM: aminoglycoside phosphotransferase; Belongs to the pseudomonas-type ThrB family. | 0.402 |
ACX96227.1 | ilvA | Hneap_1393 | Hneap_0696 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase. | 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. | 0.524 |
ACX96227.1 | ilvD | Hneap_1393 | Hneap_1151 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase. | KEGG: abo:ABO_2312 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.406 |
ACX96227.1 | ilvE | Hneap_1393 | Hneap_2135 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.854 |
ACX96227.1 | thrB | Hneap_1393 | Hneap_1690 | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase. | KEGG: tcx:Tcr_0043 homoserine kinase; TIGRFAM: homoserine kinase; PFAM: aminoglycoside phosphotransferase; Belongs to the pseudomonas-type ThrB family. | 0.925 |
ACX96950.1 | ACX96951.1 | Hneap_2133 | Hneap_2134 | Hypothetical protein. | KEGG: tgr:Tgr7_0466 hypothetical protein. | 0.746 |
ACX96950.1 | ilvE | Hneap_2133 | Hneap_2135 | Hypothetical protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.746 |
ACX96951.1 | ACX96950.1 | Hneap_2134 | Hneap_2133 | KEGG: tgr:Tgr7_0466 hypothetical protein. | Hypothetical protein. | 0.746 |
ACX96951.1 | ilvE | Hneap_2134 | Hneap_2135 | KEGG: tgr:Tgr7_0466 hypothetical protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.841 |
ilvA | ACX96227.1 | Hneap_0696 | Hneap_1393 | 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. | PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase. | 0.524 |
ilvA | ilvC | Hneap_0696 | Hneap_1900 | 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. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.686 |
ilvA | ilvD | Hneap_0696 | Hneap_1151 | 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. | KEGG: abo:ABO_2312 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.965 |
ilvA | ilvE | Hneap_0696 | Hneap_2135 | 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. | 0.904 |
ilvA | leuA | Hneap_0696 | Hneap_1576 | 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 1 subfamily. | 0.412 |
ilvC | ilvA | Hneap_1900 | Hneap_0696 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 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. | 0.686 |
ilvC | ilvD | Hneap_1900 | Hneap_1151 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | KEGG: abo:ABO_2312 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.993 |
ilvC | ilvE | Hneap_1900 | Hneap_2135 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.582 |
ilvC | leuA | Hneap_1900 | Hneap_1576 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 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 | ACX96227.1 | Hneap_1151 | Hneap_1393 | KEGG: abo:ABO_2312 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: tgr:Tgr7_1439 homoserine dehydrogenase. | 0.406 |