Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ORA67423.1 | lipA | BST25_22695 | BST25_22700 | Hypothetical protein; 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. | 0.802 |
| ORA67423.1 | lipB | BST25_22695 | BST25_22705 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate-protein ligase B; 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. | 0.802 |
| ORA67428.1 | gcvH | BST25_22720 | BST25_18645 | 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.821 |
| ORA67428.1 | gcvP | BST25_22720 | BST25_18670 | 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.832 |
| ORA67428.1 | kgd | BST25_22720 | BST25_08395 | 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Alpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
| ORA67428.1 | lipA | BST25_22720 | BST25_22700 | 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; 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. | 0.568 |
| ORA67428.1 | lipB | BST25_22720 | BST25_22705 | 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate-protein ligase B; 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. | 0.580 |
| ORA72306.1 | folE | BST25_14955 | BST25_09405 | Quinolinate synthase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | GTP cyclohydrolase I FolE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.554 |
| ORA72306.1 | lipA | BST25_14955 | BST25_22700 | Quinolinate synthase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 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. | 0.535 |
| ORA72306.1 | nadE | BST25_14955 | BST25_00640 | Quinolinate synthase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | NAD(+) synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.586 |
| ORA75162.1 | lipA | BST25_06665 | BST25_22700 | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 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. | 0.684 |
| ORA75162.1 | lipB | BST25_06665 | BST25_22705 | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Lipoate-protein ligase B; 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. | 0.705 |
| folE | ORA72306.1 | BST25_09405 | BST25_14955 | GTP cyclohydrolase I FolE; Derived by automated computational analysis using gene prediction method: Protein Homology. | Quinolinate synthase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 0.554 |
| folE | gcvP | BST25_09405 | BST25_18670 | GTP cyclohydrolase I FolE; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.448 |
| folE | lipA | BST25_09405 | BST25_22700 | GTP cyclohydrolase I FolE; 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. | 0.535 |
| folE | nadE | BST25_09405 | BST25_00640 | GTP cyclohydrolase I FolE; Derived by automated computational analysis using gene prediction method: Protein Homology. | NAD(+) synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.488 |
| gcvH | ORA67428.1 | BST25_18645 | BST25_22720 | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.821 |
| gcvH | gcvP | BST25_18645 | BST25_18670 | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.999 |
| gcvH | kgd | BST25_18645 | BST25_08395 | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Alpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.969 |
| gcvH | lipA | BST25_18645 | BST25_22700 | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 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. | 0.953 |
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