| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gltB | ilvA | ABO_2229 | ABO_2605 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 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. | 0.680 |
| gltB | ilvB-1 | ABO_2229 | ABO_0481 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | Acetolactate synthase, large subunit; Identified by sequence similarity; putative InterPro: Acetolactate synthase large subunit biosynthetic type; High confidence in function and specificity. | 0.620 |
| gltB | ilvB-2 | ABO_2229 | ABO_0704 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | Acetolactate synthase, large subunit; Identified by sequence similarity; putative InterPro: Thiamine pyrophosphate dependent enzyme; High confidence in function and specificity; Belongs to the TPP enzyme family. | 0.620 |
| gltB | ilvC | ABO_2229 | ABO_0485 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 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. | 0.734 |
| gltB | ilvD-1 | ABO_2229 | ABO_0180 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.675 |
| gltB | ilvD2 | ABO_2229 | ABO_2312 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | Dihydroxy-acid dehydratase; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.675 |
| gltB | ilvN | ABO_2229 | ABO_0482 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | Acetolactate synthase, small subunit; Identified by sequence similarity; putative identified by match to TIGR protein family HMMTIGR00119 InterPro: Acetolactate synthase small subunit; High confidence in function and specificity. | 0.678 |
| gltB | leuC | ABO_2229 | ABO_1470 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.665 |
| gltB | leuD | ABO_2229 | ABO_1469 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.616 |
| gltB | pheA | ABO_2229 | ABO_1749 | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | (P-protein including chorismate mutase and prephenate dehydratase) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF01817 InterPro: Prephenate dehydratase (PDT); High confidence in function and specificity. | 0.581 |
| ilvA | gltB | ABO_2605 | ABO_2229 | 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. | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 0.680 |
| ilvA | ilvB-1 | ABO_2605 | ABO_0481 | 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. | Acetolactate synthase, large subunit; Identified by sequence similarity; putative InterPro: Acetolactate synthase large subunit biosynthetic type; High confidence in function and specificity. | 0.947 |
| ilvA | ilvB-2 | ABO_2605 | ABO_0704 | 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. | Acetolactate synthase, large subunit; Identified by sequence similarity; putative InterPro: Thiamine pyrophosphate dependent enzyme; High confidence in function and specificity; Belongs to the TPP enzyme family. | 0.947 |
| ilvA | ilvC | ABO_2605 | ABO_0485 | 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. | 0.661 |
| ilvA | ilvD-1 | ABO_2605 | ABO_0180 | 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. | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.759 |
| ilvA | ilvD2 | ABO_2605 | ABO_2312 | 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. | Dihydroxy-acid dehydratase; (ilvD-2) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00920 InterPro: Dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.870 |
| ilvA | ilvN | ABO_2605 | ABO_0482 | 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. | Acetolactate synthase, small subunit; Identified by sequence similarity; putative identified by match to TIGR protein family HMMTIGR00119 InterPro: Acetolactate synthase small subunit; High confidence in function and specificity. | 0.964 |
| ilvA | leuC | ABO_2605 | ABO_1470 | 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. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.454 |
| ilvA | leuD | ABO_2605 | ABO_1469 | 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. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.525 |
| ilvA | pheA | ABO_2605 | ABO_1749 | 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. | (P-protein including chorismate mutase and prephenate dehydratase) identified by sequence similarity; putative identified by match to PFAM protein family HMMPF01817 InterPro: Prephenate dehydratase (PDT); High confidence in function and specificity. | 0.585 |
