node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Pnap_0111 | Pnap_1717 | Pnap_0111 | Pnap_1717 | L-threonine ammonia-lyase; 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. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2317 acetolactate synthase, large subunit, biosynthetic type. | 0.942 |
Pnap_0111 | Pnap_1718 | Pnap_0111 | Pnap_1718 | L-threonine ammonia-lyase; 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. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: pol:Bpro_2318 acetolactate synthase, small subunit. | 0.967 |
Pnap_0111 | Pnap_2213 | Pnap_0111 | Pnap_2213 | L-threonine ammonia-lyase; 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. | Transcriptional regulator, Fis family; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2817 thiamine pyrophosphate enzyme-like TPP-binding; Belongs to the TPP enzyme family. | 0.942 |
Pnap_0111 | Pnap_3336 | Pnap_0111 | Pnap_3336 | L-threonine ammonia-lyase; 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. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_0952 pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.927 |
Pnap_0111 | ilvA | Pnap_0111 | Pnap_0644 | L-threonine ammonia-lyase; 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. | L-threonine ammonia-lyase; 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. | 0.917 |
Pnap_0111 | ilvC | Pnap_0111 | Pnap_1719 | L-threonine ammonia-lyase; 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. | 0.657 |
Pnap_0111 | leuB | Pnap_0111 | Pnap_3041 | L-threonine ammonia-lyase; 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. | 0.945 |
Pnap_0600 | Pnap_1016 | Pnap_0600 | Pnap_1016 | PFAM: Dimethylmenaquinone methyltransferase; KEGG: rso:RS03175 putative transferase protein. | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | 0.612 |
Pnap_0600 | Pnap_1717 | Pnap_0600 | Pnap_1717 | PFAM: Dimethylmenaquinone methyltransferase; KEGG: rso:RS03175 putative transferase protein. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2317 acetolactate synthase, large subunit, biosynthetic type. | 0.900 |
Pnap_0600 | Pnap_1718 | Pnap_0600 | Pnap_1718 | PFAM: Dimethylmenaquinone methyltransferase; KEGG: rso:RS03175 putative transferase protein. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: pol:Bpro_2318 acetolactate synthase, small subunit. | 0.900 |
Pnap_0600 | Pnap_2213 | Pnap_0600 | Pnap_2213 | PFAM: Dimethylmenaquinone methyltransferase; KEGG: rso:RS03175 putative transferase protein. | Transcriptional regulator, Fis family; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2817 thiamine pyrophosphate enzyme-like TPP-binding; Belongs to the TPP enzyme family. | 0.900 |
Pnap_0600 | leuB | Pnap_0600 | Pnap_3041 | PFAM: Dimethylmenaquinone methyltransferase; KEGG: rso:RS03175 putative transferase protein. | 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. | 0.504 |
Pnap_1016 | Pnap_0600 | Pnap_1016 | Pnap_0600 | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | PFAM: Dimethylmenaquinone methyltransferase; KEGG: rso:RS03175 putative transferase protein. | 0.612 |
Pnap_1016 | Pnap_1632 | Pnap_1016 | Pnap_1632 | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | KEGG: pol:Bpro_3066 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | 0.906 |
Pnap_1016 | Pnap_1717 | Pnap_1016 | Pnap_1717 | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2317 acetolactate synthase, large subunit, biosynthetic type. | 0.951 |
Pnap_1016 | Pnap_1718 | Pnap_1016 | Pnap_1718 | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: pol:Bpro_2318 acetolactate synthase, small subunit. | 0.968 |
Pnap_1016 | Pnap_2213 | Pnap_1016 | Pnap_2213 | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | Transcriptional regulator, Fis family; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2817 thiamine pyrophosphate enzyme-like TPP-binding; Belongs to the TPP enzyme family. | 0.931 |
Pnap_1016 | ilvC | Pnap_1016 | Pnap_1719 | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | 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. | 0.698 |
Pnap_1632 | Pnap_1016 | Pnap_1632 | Pnap_1016 | KEGG: pol:Bpro_3066 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | KEGG: rfr:Rfer_0845 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | 0.906 |
Pnap_1632 | Pnap_1717 | Pnap_1632 | Pnap_1717 | KEGG: pol:Bpro_3066 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: pol:Bpro_2317 acetolactate synthase, large subunit, biosynthetic type. | 0.950 |