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 |
| allC | allD | b0516 | b0517 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | 0.969 |
| allC | allE | b0516 | b0515 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | 0.999 |
| allD | allC | b0517 | b0516 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | 0.969 |
| allD | allE | b0517 | b0515 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | 0.997 |
| allE | allC | b0515 | b0516 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | 0.999 |
| allE | allD | b0515 | b0517 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | 0.997 |