| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| OOR89870.1 | OOR89871.1 | B0182_06890 | B0182_06900 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.474 |
| OOR89870.1 | OOR89881.1 | B0182_06890 | B0182_06895 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | 0.528 |
| OOR89870.1 | ilvA | B0182_06890 | B0182_06915 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Threonine ammonia-lyase, 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. | 0.440 |
| OOR89870.1 | mboIIM | B0182_06890 | B0182_06905 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Site-specific DNA-methyltransferase; This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme. | 0.474 |
| OOR89870.1 | mboIIR | B0182_06890 | B0182_06910 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Recognizes the double-stranded sequences GAAGA and TCTTC and cleaves respectively 13 bases after G-1 and 7 bases before T-1, leaving a single 3' protruding nucleotide. | 0.471 |
| OOR89871.1 | OOR89870.1 | B0182_06900 | B0182_06890 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.474 |
| OOR89871.1 | OOR89874.1 | B0182_06900 | B0182_06920 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.626 |
| OOR89871.1 | OOR89881.1 | B0182_06900 | B0182_06895 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | 0.686 |
| OOR89871.1 | ilvA | B0182_06900 | B0182_06915 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Threonine ammonia-lyase, 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. | 0.709 |
| OOR89871.1 | mboIIM | B0182_06900 | B0182_06905 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Site-specific DNA-methyltransferase; This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme. | 0.773 |
| OOR89871.1 | mboIIR | B0182_06900 | B0182_06910 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Recognizes the double-stranded sequences GAAGA and TCTTC and cleaves respectively 13 bases after G-1 and 7 bases before T-1, leaving a single 3' protruding nucleotide. | 0.768 |
| OOR89874.1 | OOR89871.1 | B0182_06920 | B0182_06900 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.626 |
| OOR89874.1 | OOR89881.1 | B0182_06920 | B0182_06895 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | 0.559 |
| OOR89874.1 | ilvA | B0182_06920 | B0182_06915 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Threonine ammonia-lyase, 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. | 0.682 |
| OOR89874.1 | mboIIM | B0182_06920 | B0182_06905 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Site-specific DNA-methyltransferase; This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme. | 0.626 |
| OOR89874.1 | mboIIR | B0182_06920 | B0182_06910 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Recognizes the double-stranded sequences GAAGA and TCTTC and cleaves respectively 13 bases after G-1 and 7 bases before T-1, leaving a single 3' protruding nucleotide. | 0.631 |
| OOR89881.1 | OOR89870.1 | B0182_06895 | B0182_06890 | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.528 |
| OOR89881.1 | OOR89871.1 | B0182_06895 | B0182_06900 | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.686 |
| OOR89881.1 | OOR89874.1 | B0182_06895 | B0182_06920 | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.559 |
| OOR89881.1 | ilvA | B0182_06895 | B0182_06915 | Restriction endonuclease subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the N(4)/N(6)-methyltransferase family. | Threonine ammonia-lyase, 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. | 0.630 |