| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ECA4224 | ilvA | ECA4224 | ECA4225 | Similar to Xanthomonas campestris hypothetical protein Xcc1550 SWALL:Q8PAD5 (EMBL:AE012256) (228 aa) fasta scores: E(): 2.8e-11, 27.6% id in 221 aa, and to Shewanella oneidensis conserved hypothetical protein so1579 SWALL:AAN54636 (EMBL:AE015603) (235 aa) fasta scores: E(): 3.3e-10, 24.65% id in 215 aa. | Threonine dehydratase biosynthetic; 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. | 0.536 |
| ECA4224 | ilvD | ECA4224 | ECA4226 | Similar to Xanthomonas campestris hypothetical protein Xcc1550 SWALL:Q8PAD5 (EMBL:AE012256) (228 aa) fasta scores: E(): 2.8e-11, 27.6% id in 221 aa, and to Shewanella oneidensis conserved hypothetical protein so1579 SWALL:AAN54636 (EMBL:AE015603) (235 aa) fasta scores: E(): 3.3e-10, 24.65% id in 215 aa. | Similar to Escherichia coli dihydroxy-acid dehydratase IlvD or b3771 SWALL:ILVD_ECOLI (SWALL:P05791) (616 aa) fasta scores: E(): 9.7e-207, 87.98% id in 616 aa; Belongs to the IlvD/Edd family. | 0.536 |
| ECA4224 | ilvE | ECA4224 | ECA4227 | Similar to Xanthomonas campestris hypothetical protein Xcc1550 SWALL:Q8PAD5 (EMBL:AE012256) (228 aa) fasta scores: E(): 2.8e-11, 27.6% id in 221 aa, and to Shewanella oneidensis conserved hypothetical protein so1579 SWALL:AAN54636 (EMBL:AE015603) (235 aa) fasta scores: E(): 3.3e-10, 24.65% id in 215 aa. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.422 |
| ilvA | ECA4224 | ECA4225 | ECA4224 | Threonine dehydratase biosynthetic; 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. | Similar to Xanthomonas campestris hypothetical protein Xcc1550 SWALL:Q8PAD5 (EMBL:AE012256) (228 aa) fasta scores: E(): 2.8e-11, 27.6% id in 221 aa, and to Shewanella oneidensis conserved hypothetical protein so1579 SWALL:AAN54636 (EMBL:AE015603) (235 aa) fasta scores: E(): 3.3e-10, 24.65% id in 215 aa. | 0.536 |
| ilvA | ilvD | ECA4225 | ECA4226 | Threonine dehydratase biosynthetic; 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. | Similar to Escherichia coli dihydroxy-acid dehydratase IlvD or b3771 SWALL:ILVD_ECOLI (SWALL:P05791) (616 aa) fasta scores: E(): 9.7e-207, 87.98% id in 616 aa; Belongs to the IlvD/Edd family. | 0.928 |
| ilvA | ilvE | ECA4225 | ECA4227 | Threonine dehydratase biosynthetic; 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.940 |
| ilvD | ECA4224 | ECA4226 | ECA4224 | Similar to Escherichia coli dihydroxy-acid dehydratase IlvD or b3771 SWALL:ILVD_ECOLI (SWALL:P05791) (616 aa) fasta scores: E(): 9.7e-207, 87.98% id in 616 aa; Belongs to the IlvD/Edd family. | Similar to Xanthomonas campestris hypothetical protein Xcc1550 SWALL:Q8PAD5 (EMBL:AE012256) (228 aa) fasta scores: E(): 2.8e-11, 27.6% id in 221 aa, and to Shewanella oneidensis conserved hypothetical protein so1579 SWALL:AAN54636 (EMBL:AE015603) (235 aa) fasta scores: E(): 3.3e-10, 24.65% id in 215 aa. | 0.536 |
| ilvD | ilvA | ECA4226 | ECA4225 | Similar to Escherichia coli dihydroxy-acid dehydratase IlvD or b3771 SWALL:ILVD_ECOLI (SWALL:P05791) (616 aa) fasta scores: E(): 9.7e-207, 87.98% id in 616 aa; Belongs to the IlvD/Edd family. | Threonine dehydratase biosynthetic; 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. | 0.928 |
| ilvD | ilvE | ECA4226 | ECA4227 | Similar to Escherichia coli dihydroxy-acid dehydratase IlvD or b3771 SWALL:ILVD_ECOLI (SWALL:P05791) (616 aa) fasta scores: E(): 9.7e-207, 87.98% id in 616 aa; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.988 |
| ilvE | ECA4224 | ECA4227 | ECA4224 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Similar to Xanthomonas campestris hypothetical protein Xcc1550 SWALL:Q8PAD5 (EMBL:AE012256) (228 aa) fasta scores: E(): 2.8e-11, 27.6% id in 221 aa, and to Shewanella oneidensis conserved hypothetical protein so1579 SWALL:AAN54636 (EMBL:AE015603) (235 aa) fasta scores: E(): 3.3e-10, 24.65% id in 215 aa. | 0.422 |
| ilvE | ilvA | ECA4227 | ECA4225 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Threonine dehydratase biosynthetic; 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. | 0.940 |
| ilvE | ilvD | ECA4227 | ECA4226 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Similar to Escherichia coli dihydroxy-acid dehydratase IlvD or b3771 SWALL:ILVD_ECOLI (SWALL:P05791) (616 aa) fasta scores: E(): 9.7e-207, 87.98% id in 616 aa; Belongs to the IlvD/Edd family. | 0.988 |