node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ilvA | ilvB1 | Rv1559 | Rv3003c | Probable threonine dehydratase IlvA; 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 (By similarity). | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | 0.972 |
ilvA | ilvB2 | Rv1559 | Rv3470c | Probable threonine dehydratase IlvA; 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 (By similarity). | Putative acetolactate synthase large subunit IlvB2; Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the TPP enzyme family. | 0.953 |
ilvA | ilvC | Rv1559 | Rv3001c | Probable threonine dehydratase IlvA; 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 (By similarity). | Ketol-acid reductoisomerase (NADP(+)); 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. It is also able to use 3-hydroxypyruvate (HP). | 0.900 |
ilvA | ilvD | Rv1559 | Rv0189c | Probable threonine dehydratase IlvA; 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 (By similarity). | Rv0189c, (MTCI28.28c), len: 575 aa. Probable ilvD,dihydroxy-acid dehydratase, similar to many e.g. ILVD_LACLA|Q02139 dihydroxy-acid dehydratase (dad) from Lactococcus lactis (subsp. lactis) (Streptococcus lactis) (570 aa), FASTA scores: opt: 1605, E(): 0, (46.0% identity in 561 aa overlap). Also similar to ML2608|MLCL622.06c|O06069|ILVD_MYCLE dihydroxy-acid dehydratase from Mycobacterium leprae (564 aa). Contains PS00886 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. Belongs to the ILVD / EDD family. Cofactor: binds 1 4FE-4S cluster (potential). | 0.946 |
ilvA | ilvG | Rv1559 | Rv1820 | Probable threonine dehydratase IlvA; 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 (By similarity). | Probable acetolactate synthase IlvG (acetohydroxy-acid synthase)(ALS); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. | 0.973 |
ilvA | ilvN | Rv1559 | Rv3002c | Probable threonine dehydratase IlvA; 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 (By similarity). | Probable acetolactate synthase (small subunit) IlvN (acetohydroxy-acid synthase) (AHAS) (ALS); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the acetolactate synthase small subunit family. | 0.991 |
ilvA | ilvX | Rv1559 | Rv3509c | Probable threonine dehydratase IlvA; 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 (By similarity). | Probable acetohydroxyacid synthase IlvX (acetolactate synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. | 0.957 |
ilvA | leuA | Rv1559 | Rv3710 | Probable threonine dehydratase IlvA; 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 (By similarity). | 2-isopropylmalate synthase LeuA (alpha-isopropylmalate synthase) (alpha-IPM synthetase) (IPMS); 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). | 0.651 |
ilvA | leuB | Rv1559 | Rv2995c | Probable threonine dehydratase IlvA; 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 (By similarity). | Probable 3-isopropylmalate dehydrogenase LeuB (beta-IPM dehydrogenase) (IMDH) (3-IPM-DH); 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. | 0.977 |
ilvA | oxcA | Rv1559 | Rv0118c | Probable threonine dehydratase IlvA; 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 (By similarity). | Rv0118c, (MTV031.12c), Len: 582 aa. Probable oxcA,oxalyl-CoA decarboxylase, highly similar to many e.g. P78093|OXC_ECOLI|7449483|B65011|YFDU|B2373|Z3637|ECS325 probable oxalyl-CoA decarboxylase from Escherichia coli (564 aa); M77128|OXAOXA_1 oxalyl-CoA decarboxylase from Oxalobacter formigenes (568 aa), FASTA scores: opt: 2124,E():0, (55.6% identity in 568 aa overlap). Also similar to mycobacterial IlvB proteins e.g. MLCB1788.46c unknown TPP-requiring enzyme from Mycobacterium leprae (548 aa); and AL0086|MLCB1788_19 from Mycobacterium leprae (548 aa),FASTA scores: opt: 831, E(): 0, (33 [...] | 0.533 |
ilvB1 | ilvA | Rv3003c | Rv1559 | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Probable threonine dehydratase IlvA; 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 (By similarity). | 0.972 |
ilvB1 | ilvB2 | Rv3003c | Rv3470c | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Putative acetolactate synthase large subunit IlvB2; Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the TPP enzyme family. | 0.949 |
ilvB1 | ilvC | Rv3003c | Rv3001c | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Ketol-acid reductoisomerase (NADP(+)); 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. It is also able to use 3-hydroxypyruvate (HP). | 0.999 |
ilvB1 | ilvD | Rv3003c | Rv0189c | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Rv0189c, (MTCI28.28c), len: 575 aa. Probable ilvD,dihydroxy-acid dehydratase, similar to many e.g. ILVD_LACLA|Q02139 dihydroxy-acid dehydratase (dad) from Lactococcus lactis (subsp. lactis) (Streptococcus lactis) (570 aa), FASTA scores: opt: 1605, E(): 0, (46.0% identity in 561 aa overlap). Also similar to ML2608|MLCL622.06c|O06069|ILVD_MYCLE dihydroxy-acid dehydratase from Mycobacterium leprae (564 aa). Contains PS00886 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. Belongs to the ILVD / EDD family. Cofactor: binds 1 4FE-4S cluster (potential). | 0.967 |
ilvB1 | ilvG | Rv3003c | Rv1820 | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Probable acetolactate synthase IlvG (acetohydroxy-acid synthase)(ALS); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. | 0.949 |
ilvB1 | ilvN | Rv3003c | Rv3002c | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Probable acetolactate synthase (small subunit) IlvN (acetohydroxy-acid synthase) (AHAS) (ALS); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the acetolactate synthase small subunit family. | 0.999 |
ilvB1 | ilvX | Rv3003c | Rv3509c | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Probable acetohydroxyacid synthase IlvX (acetolactate synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. | 0.943 |
ilvB1 | leuA | Rv3003c | Rv3710 | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | 2-isopropylmalate synthase LeuA (alpha-isopropylmalate synthase) (alpha-IPM synthetase) (IPMS); 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). | 0.980 |
ilvB1 | leuB | Rv3003c | Rv2995c | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | Probable 3-isopropylmalate dehydrogenase LeuB (beta-IPM dehydrogenase) (IMDH) (3-IPM-DH); 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. | 0.977 |
ilvB2 | ilvA | Rv3470c | Rv1559 | Putative acetolactate synthase large subunit IlvB2; Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the TPP enzyme family. | Probable threonine dehydratase IlvA; 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 (By similarity). | 0.953 |