node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
TVD_06720 | TVD_10310 | TVD_06720 | TVD_10310 | 3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | enoyl-ACP reductase; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.988 |
TVD_06720 | TVD_11555 | TVD_06720 | TVD_11555 | 3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.926 |
TVD_06720 | lipB | TVD_06720 | TVD_11025 | 3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.813 |
TVD_07545 | TVD_10600 | TVD_07545 | TVD_10600 | Ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
TVD_07545 | lipA | TVD_07545 | TVD_11020 | Ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.938 |
TVD_07545 | lipB | TVD_07545 | TVD_11025 | Ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.911 |
TVD_10310 | TVD_06720 | TVD_10310 | TVD_06720 | enoyl-ACP reductase; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.988 |
TVD_10310 | TVD_11555 | TVD_10310 | TVD_11555 | enoyl-ACP reductase; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.987 |
TVD_10310 | lipB | TVD_10310 | TVD_11025 | enoyl-ACP reductase; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.800 |
TVD_10600 | TVD_07545 | TVD_10600 | TVD_07545 | Lipoate--protein ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
TVD_10600 | lipA | TVD_10600 | TVD_11020 | Lipoate--protein ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.986 |
TVD_10600 | lipB | TVD_10600 | TVD_11025 | Lipoate--protein ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.918 |
TVD_11030 | TVD_11035 | TVD_11030 | TVD_11035 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | Cytochrome C550; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.843 |
TVD_11030 | TVD_11040 | TVD_11030 | TVD_11040 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | 0.836 |
TVD_11030 | lipA | TVD_11030 | TVD_11020 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.422 |
TVD_11030 | lipB | TVD_11030 | TVD_11025 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.902 |
TVD_11030 | rlpA | TVD_11030 | TVD_11045 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | Lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.667 |
TVD_11035 | TVD_11030 | TVD_11035 | TVD_11030 | Cytochrome C550; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | 0.843 |
TVD_11035 | TVD_11040 | TVD_11035 | TVD_11040 | Cytochrome C550; Derived by automated computational analysis using gene prediction method: Protein Homology. | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | 0.821 |
TVD_11035 | lipB | TVD_11035 | TVD_11025 | Cytochrome C550; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.845 |