| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DIP1952 | ilvB | DIP1952 | DIP1098 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 0.843 |
| DIP1952 | ilvC | DIP1952 | DIP1100 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | 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. | 0.808 |
| DIP1952 | ilvD | DIP1952 | DIP1096 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | Similar to Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.579 |
| DIP1952 | ilvH | DIP1952 | DIP1099 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | Similar to Mycobacterium tuberculosis acetolactate synthase small subunit IlvH or IlvN or Rv3002c or MT3082 or MTV012.16c SW:ILVH_MYCTU (O53249) (168 aa) fasta scores: E(): 1.3e-28, 54.77% id in 157 aa, and to Corynebacterium glutamicum (Brevibacterium flavum) acetohydroxy acid synthase, small subunit IlvN or LivS TR:Q57091 (EMBL:L09232) (172 aa) fasta scores: E(): 5.4e-47, 81.06% id in 169 aa. | 0.988 |
| DIP1952 | leuB | DIP1952 | DIP1105 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.443 |
| DIP1952 | leuC | DIP1952 | DIP1127 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.870 |
| DIP1952 | leuD | DIP1952 | DIP1128 | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | 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. | 0.880 |
| ilvA | ilvB | DIP1579 | DIP1098 | 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. | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 0.983 |
| ilvA | ilvC | DIP1579 | DIP1100 | 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. | 0.851 |
| ilvA | ilvD | DIP1579 | DIP1096 | 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. | Similar to Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.916 |
| ilvA | ilvE | DIP1579 | DIP1636 | 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. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.965 |
| ilvA | ilvH | DIP1579 | DIP1099 | 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. | Similar to Mycobacterium tuberculosis acetolactate synthase small subunit IlvH or IlvN or Rv3002c or MT3082 or MTV012.16c SW:ILVH_MYCTU (O53249) (168 aa) fasta scores: E(): 1.3e-28, 54.77% id in 157 aa, and to Corynebacterium glutamicum (Brevibacterium flavum) acetohydroxy acid synthase, small subunit IlvN or LivS TR:Q57091 (EMBL:L09232) (172 aa) fasta scores: E(): 5.4e-47, 81.06% id in 169 aa. | 0.954 |
| ilvA | leuB | DIP1579 | DIP1105 | 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 dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.962 |
| ilvA | leuC | DIP1579 | DIP1127 | 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. | 0.482 |
| ilvA | leuD | DIP1579 | DIP1128 | 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. | 0.730 |
| ilvB | DIP1952 | DIP1098 | DIP1952 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | Similar to Escherichia coli pyruvate dehydrogenase [cytochrome] PoxB SW:POXB_ECOLI (P07003) (572 aa) fasta scores: E(): 1.2e-100, 45.89% id in 573 aa, and to Streptomyces coelicolor pyruvate dehydrogenase SC1A9.19 TR:Q9ZBT3 (EMBL:AL034446) (580 aa) fasta scores: E(): 1.4e-132, 56.62% id in 581 aa; Belongs to the TPP enzyme family. | 0.843 |
| ilvB | ilvA | DIP1098 | DIP1579 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 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. | 0.983 |
| ilvB | ilvC | DIP1098 | DIP1100 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 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. | 0.999 |
| ilvB | ilvD | DIP1098 | DIP1096 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | Similar to Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.981 |
| ilvB | ilvE | DIP1098 | DIP1636 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.725 |
