| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EHA62009.1 | EHA63015.1 | Syn8016DRAFT_2081 | Syn8016DRAFT_0056 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.651 |
| EHA62009.1 | EHA64196.1 | Syn8016DRAFT_2081 | Syn8016DRAFT_1239 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding. | 0.804 |
| EHA62009.1 | ilvA | Syn8016DRAFT_2081 | Syn8016DRAFT_0484 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | 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. | 0.902 |
| EHA62009.1 | ilvD | Syn8016DRAFT_2081 | Syn8016DRAFT_0903 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; HAMAP: Dihydroxy-acid dehydratase; KEGG: pmt:PMT0560 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.954 |
| EHA62009.1 | ilvE | Syn8016DRAFT_2081 | Syn8016DRAFT_0431 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.825 |
| EHA62009.1 | leuA | Syn8016DRAFT_2081 | Syn8016DRAFT_0126 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | 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. | 0.964 |
| EHA62009.1 | panB | Syn8016DRAFT_2081 | Syn8016DRAFT_2495 | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | 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. | 0.841 |
| EHA62198.1 | ilvD | Syn8016DRAFT_1493 | Syn8016DRAFT_0903 | PFAM: KDPG/KHG aldolase; KEGG: pmt:PMT1797 aldolase. | PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; HAMAP: Dihydroxy-acid dehydratase; KEGG: pmt:PMT0560 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.874 |
| EHA63015.1 | EHA62009.1 | Syn8016DRAFT_0056 | Syn8016DRAFT_2081 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | 0.651 |
| EHA63015.1 | EHA64196.1 | Syn8016DRAFT_0056 | Syn8016DRAFT_1239 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding. | 0.999 |
| EHA63015.1 | ilvA | Syn8016DRAFT_0056 | Syn8016DRAFT_0484 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 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. | 0.938 |
| EHA63015.1 | ilvC | Syn8016DRAFT_0056 | Syn8016DRAFT_2500 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 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. | 0.996 |
| EHA63015.1 | ilvD | Syn8016DRAFT_0056 | Syn8016DRAFT_0903 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; HAMAP: Dihydroxy-acid dehydratase; KEGG: pmt:PMT0560 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.921 |
| EHA63015.1 | ilvE | Syn8016DRAFT_0056 | Syn8016DRAFT_0431 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.651 |
| EHA63015.1 | leuA | Syn8016DRAFT_0056 | Syn8016DRAFT_0126 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 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. | 0.976 |
| EHA63015.1 | leuC | Syn8016DRAFT_0056 | Syn8016DRAFT_1549 | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.902 |
| EHA64196.1 | EHA62009.1 | Syn8016DRAFT_1239 | Syn8016DRAFT_2081 | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding. | PFAM: Aminotransferase, class IV; KEGG: pmt:PMT2224 aminotransferase class-IV. | 0.804 |
| EHA64196.1 | EHA63015.1 | Syn8016DRAFT_1239 | Syn8016DRAFT_0056 | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding. | TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.999 |
| EHA64196.1 | ilvA | Syn8016DRAFT_1239 | Syn8016DRAFT_0484 | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding. | 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. | 0.947 |
| EHA64196.1 | ilvC | Syn8016DRAFT_1239 | Syn8016DRAFT_2500 | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding. | 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. | 0.995 |