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 |
| STY0683 | STY0686 | gene:17584691 | gene:17584693 | Lipoic acid synthetase; 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. | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 0.999 |
| STY0683 | STY3209 | gene:17584691 | gene:17587084 | Lipoic acid synthetase; 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. | Glycine dehydrogenase (decarboxylating); 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. | 0.648 |
| STY0683 | STY3210 | gene:17584691 | gene:17587085 | Lipoic acid synthetase; 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. | Glycine cleavage system H protein; 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. | 0.932 |
| STY0683 | STY4285 | gene:17584691 | gene:17588116 | Lipoic acid synthetase; 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. | Conserved hypothetical protein; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | 0.512 |
| STY0683 | lplA | gene:17584691 | gene:17588741 | Lipoic acid synthetase; 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. | Lipoate-protein ligase A; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. | 0.980 |
| STY0686 | STY0683 | gene:17584693 | gene:17584691 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Lipoic acid synthetase; 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. | 0.999 |
| STY0686 | STY0687 | gene:17584693 | gene:17584694 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Conserved hypothetical protein; Orthologue of E. coli ybeD (YBED_ECOLI); Fasta hit to YBED_ECOLI (87 aa), 98% identity in 87 aa overlap; Belongs to the UPF0250 family. | 0.777 |
| STY0686 | STY1236 | gene:17584693 | gene:17585201 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.816 |
| STY0686 | STY1352 | gene:17584693 | gene:17585311 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Enoyl-[acyl-carrier-protein] reductase (NADH); Orthologue of E. coli fabI (FABI_ECOLI); Fasta hit to FABI_ECOLI (261 aa), 98% identity in 261 aa overlap. | 0.800 |
| STY0686 | STY2609 | gene:17584693 | gene:17586507 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 3-oxoacyl-[acyl-carrier-protein] synthase I; Fasta hit to FABF_ECOLI (412 aa), 38% identity in 417 aa overlap; Orthologue of E. coli fabB (FABB_ECOLI); Fasta hit to FABB_ECOLI (406 aa), 97% identity in 404 aa overlap; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.816 |
| STY0686 | STY3209 | gene:17584693 | gene:17587084 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Glycine dehydrogenase (decarboxylating); 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. | 0.735 |
| STY0686 | STY3210 | gene:17584693 | gene:17587085 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Glycine cleavage system H protein; 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. | 0.903 |
| STY0686 | STY4285 | gene:17584693 | gene:17588116 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Conserved hypothetical protein; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | 0.798 |
| STY0686 | lplA | gene:17584693 | gene:17588741 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Lipoate-protein ligase A; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. | 0.932 |
| STY0686 | sgaT | gene:17584693 | gene:17588560 | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | Putative transport protein SgaT; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. | 0.730 |
| STY0687 | STY0686 | gene:17584694 | gene:17584693 | Conserved hypothetical protein; Orthologue of E. coli ybeD (YBED_ECOLI); Fasta hit to YBED_ECOLI (87 aa), 98% identity in 87 aa overlap; Belongs to the UPF0250 family. | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 0.777 |
| STY1236 | STY0686 | gene:17585201 | gene:17584693 | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 0.816 |
| STY1236 | STY1352 | gene:17585201 | gene:17585311 | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Enoyl-[acyl-carrier-protein] reductase (NADH); Orthologue of E. coli fabI (FABI_ECOLI); Fasta hit to FABI_ECOLI (261 aa), 98% identity in 261 aa overlap. | 0.994 |
| STY1236 | STY2609 | gene:17585201 | gene:17586507 | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 3-oxoacyl-[acyl-carrier-protein] synthase I; Fasta hit to FABF_ECOLI (412 aa), 38% identity in 417 aa overlap; Orthologue of E. coli fabB (FABB_ECOLI); Fasta hit to FABB_ECOLI (406 aa), 97% identity in 404 aa overlap; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.915 |
| STY1352 | STY0686 | gene:17585311 | gene:17584693 | Enoyl-[acyl-carrier-protein] reductase (NADH); Orthologue of E. coli fabI (FABI_ECOLI); Fasta hit to FABI_ECOLI (261 aa), 98% identity in 261 aa overlap. | Lipoate-protein ligase B (lipoate biosynthesis protein 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. | 0.800 |
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