node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ERJ18355.1 | ERJ18356.1 | SSPSH_002815 | SSPSH_002816 | Homoserine O-acetyltransferase protein; Overlaps another CDS with the same product name. | Hypothetical protein. | 0.724 |
ERJ18355.1 | ilvA1 | SSPSH_002815 | SSPSH_002811 | Homoserine O-acetyltransferase protein; Overlaps another CDS with the same product name. | Threonine dehydratase biosynthetic protein; 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. | 0.596 |
ERJ18355.1 | metX | SSPSH_002815 | SSPSH_002814 | Homoserine O-acetyltransferase protein; Overlaps another CDS with the same product name. | Homoserine O-acetyltransferase protein; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. | 0.997 |
ERJ18355.1 | proC | SSPSH_002815 | SSPSH_002812 | Homoserine O-acetyltransferase protein; Overlaps another CDS with the same product name. | Pyrroline-5-carboxylate reductase protein; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.801 |
ERJ18355.1 | yggT | SSPSH_002815 | SSPSH_002813 | Homoserine O-acetyltransferase protein; Overlaps another CDS with the same product name. | Putative inner membrane protein. | 0.801 |
ERJ18356.1 | ERJ18355.1 | SSPSH_002816 | SSPSH_002815 | Hypothetical protein. | Homoserine O-acetyltransferase protein; Overlaps another CDS with the same product name. | 0.724 |
ERJ18356.1 | ilvA1 | SSPSH_002816 | SSPSH_002811 | Hypothetical protein. | Threonine dehydratase biosynthetic protein; 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. | 0.487 |
ERJ18356.1 | metX | SSPSH_002816 | SSPSH_002814 | Hypothetical protein. | Homoserine O-acetyltransferase protein; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. | 0.702 |
ERJ18356.1 | proC | SSPSH_002816 | SSPSH_002812 | Hypothetical protein. | Pyrroline-5-carboxylate reductase protein; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.724 |
ERJ18356.1 | yggT | SSPSH_002816 | SSPSH_002813 | Hypothetical protein. | Putative inner membrane protein. | 0.757 |
ERJ20696.1 | yafS | SSPSH_000033 | SSPSH_001600 | 3-dehydroquinate dehydratase I protein. | Putative SAM-dependent methyltransferase protein. | 0.662 |
ERJ20696.1 | yggT | SSPSH_000033 | SSPSH_002813 | 3-dehydroquinate dehydratase I protein. | Putative inner membrane protein. | 0.568 |
ERJ20826.1 | proC | SSPSH_000168 | SSPSH_002812 | Alanine racemase domain-containing protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Pyrroline-5-carboxylate reductase protein; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.896 |
ERJ20826.1 | yggT | SSPSH_000168 | SSPSH_002813 | Alanine racemase domain-containing protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Putative inner membrane protein. | 0.724 |
ftsZ | gatB | SSPSH_000306 | SSPSH_003179 | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Aspartyl-glutamyl-tRNA amidotransferase subunit B protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.673 |
ftsZ | yggT | SSPSH_000306 | SSPSH_002813 | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Putative inner membrane protein. | 0.719 |
gatB | ftsZ | SSPSH_003179 | SSPSH_000306 | Aspartyl-glutamyl-tRNA amidotransferase subunit B protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.673 |
gatB | yggT | SSPSH_003179 | SSPSH_002813 | Aspartyl-glutamyl-tRNA amidotransferase subunit B protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | Putative inner membrane protein. | 0.647 |
ilvA1 | ERJ18355.1 | SSPSH_002811 | SSPSH_002815 | Threonine dehydratase biosynthetic protein; 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 O-acetyltransferase protein; Overlaps another CDS with the same product name. | 0.596 |
ilvA1 | ERJ18356.1 | SSPSH_002811 | SSPSH_002816 | Threonine dehydratase biosynthetic protein; 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. | Hypothetical protein. | 0.487 |