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 |
| DR97_667 | DR97_668 | DR97_667 | DR97_668 | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | 0.802 |
| DR97_667 | DR97_669 | DR97_667 | DR97_669 | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | annotation not available | 0.705 |
| DR97_667 | DR97_672 | DR97_667 | DR97_672 | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | annotation not available | 0.737 |
| DR97_667 | DR97_682 | DR97_667 | DR97_682 | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | Trans-L-3-hydroxyproline dehydratase; Probably catalyzes the dehydration of trans-3-hydroxy-L- proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source . Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor proline racemase activity | 0.705 |
| DR97_667 | DR97_683 | DR97_667 | DR97_683 | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | 1-pyrroline-4-hydroxy-2-carboxylate deaminase; Belongs to the DapA family | 0.472 |
| DR97_667 | Ferredoxin | DR97_667 | DR97_670 | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | annotation not available | 0.742 |
| DR97_668 | DR97_667 | DR97_668 | DR97_667 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | 0.802 |
| DR97_668 | DR97_669 | DR97_668 | DR97_669 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | annotation not available | 0.997 |
| DR97_668 | DR97_672 | DR97_668 | DR97_672 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | annotation not available | 0.996 |
| DR97_668 | DR97_676 | DR97_668 | DR97_676 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | annotation not available | 0.833 |
| DR97_668 | DR97_682 | DR97_668 | DR97_682 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | Trans-L-3-hydroxyproline dehydratase; Probably catalyzes the dehydration of trans-3-hydroxy-L- proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source . Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor proline racemase activity | 0.442 |
| DR97_668 | DR97_683 | DR97_668 | DR97_683 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | 1-pyrroline-4-hydroxy-2-carboxylate deaminase; Belongs to the DapA family | 0.971 |
| DR97_668 | Ferredoxin | DR97_668 | DR97_670 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | annotation not available | 0.996 |
| DR97_668 | lhpD | DR97_668 | DR97_685 | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | Malate/l-lactate dehydrogenase family protein; Catalyzes the reduction of both Delta(1)-pyrroline-2- carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to L-proline and L-pipecolate, respectively, using NADPH as the electron donor. Cannot use NADH instead of NADPH. Is likely involved in a degradation pathway that converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source. Can also catalyze the reverse oxidation reactions, albeit at a much lower rate. Is also able to use Delta(1)-pyrroline- (4S)-hydr [...] | 0.821 |
| DR97_669 | DR97_667 | DR97_669 | DR97_667 | annotation not available | Putative transcriptional regulator; Iron dependent repressor, N-terminal DNA binding domain protein | 0.705 |
| DR97_669 | DR97_668 | DR97_669 | DR97_668 | annotation not available | 4-hydroxyproline epimerase; Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate | 0.997 |
| DR97_669 | DR97_672 | DR97_669 | DR97_672 | annotation not available | annotation not available | 0.995 |
| DR97_669 | DR97_676 | DR97_669 | DR97_676 | annotation not available | annotation not available | 0.788 |
| DR97_669 | DR97_682 | DR97_669 | DR97_682 | annotation not available | Trans-L-3-hydroxyproline dehydratase; Probably catalyzes the dehydration of trans-3-hydroxy-L- proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source . Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor proline racemase activity | 0.686 |
| DR97_669 | DR97_683 | DR97_669 | DR97_683 | annotation not available | 1-pyrroline-4-hydroxy-2-carboxylate deaminase; Belongs to the DapA family | 0.978 |
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