node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EIG53450.1 | EIG53511.1 | DesU5LDRAFT_1770 | DesU5LDRAFT_1834 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | PFAM: ACT domain; Small subunit of acetolactate synthase. | 0.829 |
EIG53450.1 | EIG54382.1 | DesU5LDRAFT_1770 | DesU5LDRAFT_2737 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | Threonine dehydratase, medium form; 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. | 0.952 |
EIG53450.1 | EIG55162.1 | DesU5LDRAFT_1770 | DesU5LDRAFT_3541 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | Acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 0.872 |
EIG53450.1 | EIG55653.1 | DesU5LDRAFT_1770 | DesU5LDRAFT_4057 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | NAD-dependent aldehyde dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family. | 0.915 |
EIG53450.1 | rpsI | DesU5LDRAFT_1770 | DesU5LDRAFT_3276 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | PFAM: Ribosomal protein S9/S16; Belongs to the universal ribosomal protein uS9 family. | 0.644 |
EIG53450.1 | rpsP | DesU5LDRAFT_1770 | DesU5LDRAFT_2823 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | PFAM: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family. | 0.407 |
EIG53511.1 | EIG53450.1 | DesU5LDRAFT_1834 | DesU5LDRAFT_1770 | PFAM: ACT domain; Small subunit of acetolactate synthase. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | 0.829 |
EIG53511.1 | EIG53942.1 | DesU5LDRAFT_1834 | DesU5LDRAFT_2276 | PFAM: ACT domain; Small subunit of acetolactate synthase. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.761 |
EIG53511.1 | EIG54382.1 | DesU5LDRAFT_1834 | DesU5LDRAFT_2737 | PFAM: ACT domain; Small subunit of acetolactate synthase. | Threonine dehydratase, medium form; 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. | 0.983 |
EIG53511.1 | EIG55162.1 | DesU5LDRAFT_1834 | DesU5LDRAFT_3541 | PFAM: ACT domain; Small subunit of acetolactate synthase. | Acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 0.998 |
EIG53511.1 | EIG55653.1 | DesU5LDRAFT_1834 | DesU5LDRAFT_4057 | PFAM: ACT domain; Small subunit of acetolactate synthase. | NAD-dependent aldehyde dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family. | 0.723 |
EIG53942.1 | EIG53511.1 | DesU5LDRAFT_2276 | DesU5LDRAFT_1834 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | PFAM: ACT domain; Small subunit of acetolactate synthase. | 0.761 |
EIG53942.1 | EIG54382.1 | DesU5LDRAFT_2276 | DesU5LDRAFT_2737 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | Threonine dehydratase, medium form; 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 |
EIG53942.1 | EIG55162.1 | DesU5LDRAFT_2276 | DesU5LDRAFT_3541 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | Acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 0.414 |
EIG54382.1 | EIG53450.1 | DesU5LDRAFT_2737 | DesU5LDRAFT_1770 | Threonine dehydratase, medium form; 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. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | 0.952 |
EIG54382.1 | EIG53511.1 | DesU5LDRAFT_2737 | DesU5LDRAFT_1834 | Threonine dehydratase, medium form; 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. | PFAM: ACT domain; Small subunit of acetolactate synthase. | 0.983 |
EIG54382.1 | EIG53942.1 | DesU5LDRAFT_2737 | DesU5LDRAFT_2276 | Threonine dehydratase, medium form; 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. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.965 |
EIG54382.1 | EIG55162.1 | DesU5LDRAFT_2737 | DesU5LDRAFT_3541 | Threonine dehydratase, medium form; 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, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 0.937 |
EIG54382.1 | EIG55653.1 | DesU5LDRAFT_2737 | DesU5LDRAFT_4057 | Threonine dehydratase, medium form; 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. | NAD-dependent aldehyde dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family. | 0.954 |
EIG54382.1 | rplC | DesU5LDRAFT_2737 | DesU5LDRAFT_3619 | Threonine dehydratase, medium form; 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. | 50S ribosomal protein L3, bacterial; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family. | 0.946 |