node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
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 | ilvE | RB8510 | RB5738 | 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. | PMID: 3897211 best DB hits: BLAST: swissprot:Q58414; ILVE_METJA PUTATIVE BRANCHED-CHAIN AMINO ACID; E=3e-07 gb:AAB90305.1; (AE001039) branched-chain amino acid; E=2e-05 pir:F69057; branched-chain amino-acid aminotransferase -; E=6e-05 COG: MJ1008; COG0115 Branched-chain amino acid; E=3e-08. | 0.871 |
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 | metB | RB8510 | RB6442 | 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. | Cystathionine gamma-synthase; PMID: 9002610 best DB hits: BLAST: embl:CAA64383.1; (X94756) cystathionine gamma-synthase; E=2e-75 gb:AAF26162.1; AC008261_19 (AC008261) putative cystathionine; E=2e-75 swissprot:P55217; METB_ARATH CYSTATHIONINE GAMMA-SYNTHASE,; E=3e-75 COG: APE1226; COG0626 Cystathionine beta-lyases/cystathionine; E=1e-64 PA5025; COG2873 O-acetylhomoserine sulfhydrylase; E=4e-47 PH1093; COG0626 Cystathionine beta-lyases/cystathionine; E=5e-47 PFAM: PF01053; Cys/Met metabolism PLP-depend; E=4.5e-154. | 0.869 |
hom | metB-2 | RB8510 | RB6443 | 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. | Cystathionine gamma-lyase homolog; PMID: 9843488 best DB hits: BLAST: pir:T45483; cystathionine gamma-lyase homolog [imported] -; E=9e-93 pir:F83595; probable cystathionine gamma-lyase PA0400 [imported] -; E=1e-92 gb:AAG19548.1; (AE005045) cystathionine alpha synthase; MetB; E=3e-92 COG: PA0400; COG0626 Cystathionine beta-lyases/cystathionine; E=1e-93 PFAM: PF01053; Cys/Met metabolism PLP-depend; E=2.9e-199. | 0.869 |
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 | 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 | ilvD-3 | RB5151 | RB1480 | 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: 8688087 best DB hits: BLAST: pir:T36902; probable dihydroxy-acid dehydratase - Streptomyces; E=1e-172 embl:CAB61588.1; (AL133210) putative dihydroxy-acid dehydratase; E=1e-132 swissprot:Q58672; ILVD_METJA DIHYDROXY-ACID DEHYDRATASE (DAD); E=4e-79 COG: MJ1276; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=4e-80 ilvD; COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; E=1e-51 XF0099; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=1e-50 PFAM: PF00920; Dehydratase family; E=1.2e-108; Belongs to the IlvD/Edd family. | 0.767 |
ilvA | ilvE | RB5151 | RB5738 | 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. | PMID: 3897211 best DB hits: BLAST: swissprot:Q58414; ILVE_METJA PUTATIVE BRANCHED-CHAIN AMINO ACID; E=3e-07 gb:AAB90305.1; (AE001039) branched-chain amino acid; E=2e-05 pir:F69057; branched-chain amino-acid aminotransferase -; E=6e-05 COG: MJ1008; COG0115 Branched-chain amino acid; E=3e-08. | 0.884 |
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 |
ilvA | metB | RB5151 | RB6442 | 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. | Cystathionine gamma-synthase; PMID: 9002610 best DB hits: BLAST: embl:CAA64383.1; (X94756) cystathionine gamma-synthase; E=2e-75 gb:AAF26162.1; AC008261_19 (AC008261) putative cystathionine; E=2e-75 swissprot:P55217; METB_ARATH CYSTATHIONINE GAMMA-SYNTHASE,; E=3e-75 COG: APE1226; COG0626 Cystathionine beta-lyases/cystathionine; E=1e-64 PA5025; COG2873 O-acetylhomoserine sulfhydrylase; E=4e-47 PH1093; COG0626 Cystathionine beta-lyases/cystathionine; E=5e-47 PFAM: PF01053; Cys/Met metabolism PLP-depend; E=4.5e-154. | 0.843 |
ilvA | metB-2 | RB5151 | RB6443 | 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. | Cystathionine gamma-lyase homolog; PMID: 9843488 best DB hits: BLAST: pir:T45483; cystathionine gamma-lyase homolog [imported] -; E=9e-93 pir:F83595; probable cystathionine gamma-lyase PA0400 [imported] -; E=1e-92 gb:AAG19548.1; (AE005045) cystathionine alpha synthase; MetB; E=3e-92 COG: PA0400; COG0626 Cystathionine beta-lyases/cystathionine; E=1e-93 PFAM: PF01053; Cys/Met metabolism PLP-depend; E=2.9e-199. | 0.843 |
ilvD-2 | ilvA | RB12087 | RB5151 | 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; [...] | 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. | 0.887 |
ilvD-2 | ilvE | RB12087 | RB5738 | 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; [...] | PMID: 3897211 best DB hits: BLAST: swissprot:Q58414; ILVE_METJA PUTATIVE BRANCHED-CHAIN AMINO ACID; E=3e-07 gb:AAB90305.1; (AE001039) branched-chain amino acid; E=2e-05 pir:F69057; branched-chain amino-acid aminotransferase -; E=6e-05 COG: MJ1008; COG0115 Branched-chain amino acid; E=3e-08. | 0.965 |
ilvD-2 | ilvE-2 | RB12087 | RB8126 | 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; [...] | Putative branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.965 |
ilvD-2 | leuA-2 | RB12087 | RB12756 | 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; [...] | 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. | 0.969 |
ilvD-2 | leuA-3 | RB12087 | RB1317 | 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; [...] | 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. | 0.958 |
ilvD-2 | panB | RB12087 | RB9090 | 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; [...] | 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. | 0.912 |
ilvD-3 | ilvA | RB1480 | RB5151 | Dihydroxy-acid dehydratase; PMID: 8688087 best DB hits: BLAST: pir:T36902; probable dihydroxy-acid dehydratase - Streptomyces; E=1e-172 embl:CAB61588.1; (AL133210) putative dihydroxy-acid dehydratase; E=1e-132 swissprot:Q58672; ILVD_METJA DIHYDROXY-ACID DEHYDRATASE (DAD); E=4e-79 COG: MJ1276; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=4e-80 ilvD; COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; E=1e-51 XF0099; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=1e-50 PFAM: PF00920; Dehydratase family; E=1.2e-108; Belongs to the IlvD/Edd family. | 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. | 0.767 |
ilvD-3 | ilvE | RB1480 | RB5738 | Dihydroxy-acid dehydratase; PMID: 8688087 best DB hits: BLAST: pir:T36902; probable dihydroxy-acid dehydratase - Streptomyces; E=1e-172 embl:CAB61588.1; (AL133210) putative dihydroxy-acid dehydratase; E=1e-132 swissprot:Q58672; ILVD_METJA DIHYDROXY-ACID DEHYDRATASE (DAD); E=4e-79 COG: MJ1276; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=4e-80 ilvD; COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; E=1e-51 XF0099; COG0129 Dihydroxyacid dehydratase/phosphogluconate; E=1e-50 PFAM: PF00920; Dehydratase family; E=1.2e-108; Belongs to the IlvD/Edd family. | PMID: 3897211 best DB hits: BLAST: swissprot:Q58414; ILVE_METJA PUTATIVE BRANCHED-CHAIN AMINO ACID; E=3e-07 gb:AAB90305.1; (AE001039) branched-chain amino acid; E=2e-05 pir:F69057; branched-chain amino-acid aminotransferase -; E=6e-05 COG: MJ1008; COG0115 Branched-chain amino acid; E=3e-08. | 0.828 |