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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| apaH | bioH | b0049 | b3412 | Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | 0.617 |
| apaH | menH | b0049 | b2263 | Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro; Belongs to the AB hydrolase superfamily. MenH family. | 0.617 |
| apaH | mhpC | b0049 | b0349 | Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | 2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6- oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain; Belongs to the AB hydrolase superfamily. MhpC family. | 0.617 |
| apaH | ybfF | b0049 | b0686 | Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | acyl-CoA esterase; Displays esterase activity toward palmitoyl-CoA, malonyl-CoA and pNP-butyrate. | 0.617 |
| bioH | apaH | b3412 | b0049 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | 0.617 |
| bioH | frsA | b3412 | b0239 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | 0.488 |
| bioH | menH | b3412 | b2263 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro; Belongs to the AB hydrolase superfamily. MenH family. | 0.699 |
| bioH | mhpC | b3412 | b0349 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | 2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6- oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain; Belongs to the AB hydrolase superfamily. MhpC family. | 0.424 |
| bioH | ybfF | b3412 | b0686 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | acyl-CoA esterase; Displays esterase activity toward palmitoyl-CoA, malonyl-CoA and pNP-butyrate. | 0.738 |
| bioH | yeiG | b3412 | b2154 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | S-formylglutathione hydrolase; Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids. | 0.528 |
| bioH | yjfP | b3412 | b4190 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | Acyl CoA esterase; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. | 0.805 |
| bioH | ypfH | b3412 | b2473 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | palmitoyl-CoA esterase activity, uncertain physiological substrate; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. | 0.571 |
| bioH | yqiA | b3412 | b3031 | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | Acyl CoA esterase; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. | 0.544 |
| frsA | bioH | b0239 | b3412 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | pimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] | 0.488 |
| frsA | menH | b0239 | b2263 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro; Belongs to the AB hydrolase superfamily. MenH family. | 0.892 |
| frsA | ybfF | b0239 | b0686 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | acyl-CoA esterase; Displays esterase activity toward palmitoyl-CoA, malonyl-CoA and pNP-butyrate. | 0.792 |
| frsA | yeiG | b0239 | b2154 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | S-formylglutathione hydrolase; Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids. | 0.663 |
| frsA | yjfP | b0239 | b4190 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | Acyl CoA esterase; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. | 0.655 |
| frsA | ypfH | b0239 | b2473 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | palmitoyl-CoA esterase activity, uncertain physiological substrate; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. | 0.828 |
| frsA | yqiA | b0239 | b3031 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | Acyl CoA esterase; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. | 0.811 |
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