node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
RB12905 | hom | RB12905 | RB8510 | 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 [...] | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | 0.486 |
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. | 0.965 |
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; [...] | 0.964 |
RB12905 | ilvE-2 | RB12905 | RB8126 | 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 [...] | Putative branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.586 |
RB12905 | leuA | RB12905 | RB12656 | 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 dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.705 |
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. | 0.939 |
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. | 0.905 |
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. | 0.970 |
RB12905 | leuD | RB12905 | RB12658 | 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 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. | 0.759 |
hom | RB12905 | RB8510 | RB12905 | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | 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 [...] | 0.486 |
hom | ilvA | RB8510 | RB5151 | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | 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. | 0.537 |
hom | ilvC | RB8510 | RB9869 | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | 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. | 0.482 |
hom | ilvE-2 | RB8510 | RB8126 | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | Putative branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.871 |
hom | leuA | RB8510 | RB12656 | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.445 |
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 [...] | 0.965 |
ilvA | hom | RB5151 | RB8510 | 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. | Homoserine dehydrogenase; PMID: 1333566 best DB hits: BLAST: pir:F69031; homoserine dehydrogenase (EC 1.1.1.3) - Methanobacterium; E=4e-81 gb:AAF21129.1; L78665_3 (L78665) homoserine dehydrogenase; E=2e-80 swissprot:P29365; DHOM_PSEAE HOMOSERINE DEHYDROGENASE (HDH); E=1e-77 COG: MTH1232; COG0460 Homoserine dehydrogenase; E=4e-82 PFAM: PF02737; 3-hydroxyacyl-CoA dehydrogenase; E=0.85 PF02254; KTN NAD-binding domain; E=0.19 PF01408; Oxidoreductase family, NAD-bind; E=0.73. | 0.537 |
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. | 0.778 |
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; [...] | 0.887 |
ilvA | ilvE-2 | RB5151 | RB8126 | 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. | Putative branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.884 |