| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RB12905 | ilvA | RB12905 | RB5151 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | Threonine dehydratase; 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. | 0.966 |
| RB12905 | ilvC | RB12905 | RB9869 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | Acetohydroxy acid isomeroreductase; 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. | 0.997 |
| RB12905 | ilvD-2 | RB12905 | RB12087 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | Dihydroxy-acid dehydratase; PMID: 8325851 PMID: 7771772 best DB hits: BLAST: ddbj:BAB03011.1; (AP001297) dihydroxy-acid dehydratase; E=0.0 swissprot:Q10318; ILV3_SCHPO PUTATIVE DIHYDROXY-ACID DEHYDRATASE,; E=0.0 embl:CAA89540.1; (Z49516) ORF YJR016c [Saccharomyces cerevisiae]; E=1e-170 COG: YJR016c; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=1e-171 ilvD; COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; E=7e-81 PA0353; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=4e-80 PFAM: PF00391; PEP-utilizing enzyme, mobile do; E=0.48 PF00920; Dehydratase family; [...] | 0.957 |
| RB12905 | ilvN | RB12905 | RB9871 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | Probable acetolactate synthase small subunit; PMID: 6308579 PMID: 1851954 best DB hits: BLAST: swissprot:O27492; ILVH_METTH PROBABLE ACETOLACTATE SYNTHASE SMALL; E=1e-27 pir:S74358; acetolactate synthase ilvN - Synechocystis sp. (strain; E=5e-27 gb:AAB89532.1; (AE000985) acetolactate synthase, small subunit; E=9e-27 COG: MTH1443; COG0440 Acetolactate synthase, small subunit; E=9e-29 PFAM: PF01842; ACT domain; E=1.1e-18. | 0.999 |
| RB12905 | korA | RB12905 | RB6935 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 2-oxoglutarate ferredoxin oxidoreductase alpha subunit; PMID: 11401501 best DB hits: BLAST: embl:CAC08296.1; (AL392148) putative oxidoreductase [Streptomyces; E=1e-165 embl:CAB60189.1; (AL132824) putative oxidoreductase alpha-subunit; E=1e-164 pir:F70864; probable oxidoreductase alpha subunit - Mycobacterium; E=1e-160 COG: Rv2455c_2; COG0674 Pyruvate:ferredoxin oxidoreductase and related; E=1e-106 Rv2455c_1; COG1014 Pyruvate:ferredoxin oxidoreductase and related; E=2e-46 BH2374_2; COG0674 Pyruvate:ferredoxin oxidoreductase and related; E=2e-40 PFAM: PF01855; Pyruvate flavodoxin/ferredo [...] | 0.947 |
| RB12905 | korB | RB12905 | RB6933 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 2-oxoglutarate ferredoxin oxidoreductase beta subunit; PMID: 11401501 best DB hits: BLAST: embl:CAC08295.1; (AL392148) putative oxidoreductase [Streptomyces; E=1e-104 embl:CAB60188.1; (AL132824) putative oxidoreductase beta-subunit; E=1e-103 pir:E70864; probable oxidoreductase - Mycobacterium tuberculosis; E=2e-94 COG: Rv2454c; COG1013 Pyruvate:ferredoxin oxidoreductase and related; E=1e-95 PFAM: PF02775; Thiamine pyrophosphate enzyme,; E=0.19. | 0.929 |
| RB12905 | leuA-2 | RB12905 | RB12756 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 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. | 0.943 |
| RB12905 | leuA-3 | RB12905 | RB1317 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 2-isopropylmalate synthase; PMID: 6171647 best DB hits: BLAST: swissprot:O66682; LY41_AQUAE PUTATIVE LYASE AQ_356 ----- pir:; E=1e-132 pir:E75045; 2-isopropylmalate synthase (leua-3) PAB0894 - Pyrococcus; E=1e-130 swissprot:Q9WZ22; LY41_THEMA PUTATIVE LYASE TM0552 ----- pir:; E=1e-124 COG: aq_356; COG0119 Isopropylmalate/homocitrate/citramalate synthases; E=1e-133 PFAM: PF00682; HMGL-like; E=6.6e-09; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.911 |
| RB12905 | leuB | RB12905 | RB12597 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 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 1 subfamily. | 0.974 |
| RB12905 | leuB-2 | RB12905 | RB3767 | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 3-isopropylmalate dehydrogenase; PMID: 3110742 best DB hits: BLAST: pir:D75045; 3-isopropylmalate dehydrogenase (leub) PAB2424 -; E=2e-52 swissprot:O66607; LEU3_AQUAE 3-ISOPROPYLMALATE DEHYDROGENASE; E=6e-51 swissprot:Q9WZ26; LEU3_THEMA 3-ISOPROPYLMALATE DEHYDROGENASE; E=2e-49 COG: PAB2424; COG0473 Isocitrate/isopropylmalate dehydrogenase; E=2e-53 PFAM: PF00180; Isocitrate and isopropylmalate dehyd; E=6.3e-108 PF02376; CUT domain; E=0.32. | 0.970 |
| ilvA | RB12905 | RB5151 | RB12905 | Threonine dehydratase; 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 III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 0.966 |
| ilvA | ilvC | RB5151 | RB9869 | Threonine dehydratase; 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. | Acetohydroxy acid isomeroreductase; 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. | 0.776 |
| ilvA | ilvD-2 | RB5151 | RB12087 | Threonine dehydratase; 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; PMID: 8325851 PMID: 7771772 best DB hits: BLAST: ddbj:BAB03011.1; (AP001297) dihydroxy-acid dehydratase; E=0.0 swissprot:Q10318; ILV3_SCHPO PUTATIVE DIHYDROXY-ACID DEHYDRATASE,; E=0.0 embl:CAA89540.1; (Z49516) ORF YJR016c [Saccharomyces cerevisiae]; E=1e-170 COG: YJR016c; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=1e-171 ilvD; COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; E=7e-81 PA0353; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=4e-80 PFAM: PF00391; PEP-utilizing enzyme, mobile do; E=0.48 PF00920; Dehydratase family; [...] | 0.874 |
| ilvA | ilvN | RB5151 | RB9871 | Threonine dehydratase; 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. | Probable acetolactate synthase small subunit; PMID: 6308579 PMID: 1851954 best DB hits: BLAST: swissprot:O27492; ILVH_METTH PROBABLE ACETOLACTATE SYNTHASE SMALL; E=1e-27 pir:S74358; acetolactate synthase ilvN - Synechocystis sp. (strain; E=5e-27 gb:AAB89532.1; (AE000985) acetolactate synthase, small subunit; E=9e-27 COG: MTH1443; COG0440 Acetolactate synthase, small subunit; E=9e-29 PFAM: PF01842; ACT domain; E=1.1e-18. | 0.956 |
| ilvA | korA | RB5151 | RB6935 | Threonine dehydratase; 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-oxoglutarate ferredoxin oxidoreductase alpha subunit; PMID: 11401501 best DB hits: BLAST: embl:CAC08296.1; (AL392148) putative oxidoreductase [Streptomyces; E=1e-165 embl:CAB60189.1; (AL132824) putative oxidoreductase alpha-subunit; E=1e-164 pir:F70864; probable oxidoreductase alpha subunit - Mycobacterium; E=1e-160 COG: Rv2455c_2; COG0674 Pyruvate:ferredoxin oxidoreductase and related; E=1e-106 Rv2455c_1; COG1014 Pyruvate:ferredoxin oxidoreductase and related; E=2e-46 BH2374_2; COG0674 Pyruvate:ferredoxin oxidoreductase and related; E=2e-40 PFAM: PF01855; Pyruvate flavodoxin/ferredo [...] | 0.473 |
| ilvA | leuB | RB5151 | RB12597 | Threonine dehydratase; 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 1 subfamily. | 0.946 |
| ilvA | leuB-2 | RB5151 | RB3767 | Threonine dehydratase; 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; PMID: 3110742 best DB hits: BLAST: pir:D75045; 3-isopropylmalate dehydrogenase (leub) PAB2424 -; E=2e-52 swissprot:O66607; LEU3_AQUAE 3-ISOPROPYLMALATE DEHYDROGENASE; E=6e-51 swissprot:Q9WZ26; LEU3_THEMA 3-ISOPROPYLMALATE DEHYDROGENASE; E=2e-49 COG: PAB2424; COG0473 Isocitrate/isopropylmalate dehydrogenase; E=2e-53 PFAM: PF00180; Isocitrate and isopropylmalate dehyd; E=6.3e-108 PF02376; CUT domain; E=0.32. | 0.947 |
| ilvC | RB12905 | RB9869 | RB12905 | Acetohydroxy acid isomeroreductase; 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. | Acetolactate synthase III [Precursor]; PMID: 1896019 best DB hits: BLAST: swissprot:P27819; ILV3_BRANA ACETOLACTATE SYNTHASE III,; E=1e-167 swissprot:P27818; ILV1_BRANA ACETOLACTATE SYNTHASE I, CHLOROPLAST; E=1e-167 pir:S15004; acetolactate synthase (EC 4.1.3.18) 2 precursor - rape; E=1e-167 COG: AF1720; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-129 ilvG; COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate; E=1e-123 slr2088; COG0028 Thiamine pyrophosphate-requiring enzymes; E=1e-121 PFAM: PF02776; Thiamine pyrophosphate enzyme,; E=9.8e-87 PF00205; Thiamine pyrop [...] | 0.997 |
| ilvC | ilvA | RB9869 | RB5151 | Acetohydroxy acid isomeroreductase; 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; 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. | 0.776 |
| ilvC | ilvD-2 | RB9869 | RB12087 | Acetohydroxy acid isomeroreductase; 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. | Dihydroxy-acid dehydratase; PMID: 8325851 PMID: 7771772 best DB hits: BLAST: ddbj:BAB03011.1; (AP001297) dihydroxy-acid dehydratase; E=0.0 swissprot:Q10318; ILV3_SCHPO PUTATIVE DIHYDROXY-ACID DEHYDRATASE,; E=0.0 embl:CAA89540.1; (Z49516) ORF YJR016c [Saccharomyces cerevisiae]; E=1e-170 COG: YJR016c; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=1e-171 ilvD; COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; E=7e-81 PA0353; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=4e-80 PFAM: PF00391; PEP-utilizing enzyme, mobile do; E=0.48 PF00920; Dehydratase family; [...] | 0.983 |