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 |
| allE | ybiB | b0515 | b0800 | 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. | Putative family 3 glycosyltransferase; Putative enzyme; Belongs to the anthranilate phosphoribosyltransferase family. | 0.505 |
| allE | ybiC | b0515 | b0801 | 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. | Putative dehydrogenase; Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. | 0.624 |
| aspC | dadA | b0928 | b1189 | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | 0.903 |
| aspC | hisC | b0928 | b2021 | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | 0.956 |
| aspC | tyrB | b0928 | b4054 | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. | 0.918 |
| aspC | ybiC | b0928 | b0801 | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | Putative dehydrogenase; Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. | 0.916 |
| dadA | aspC | b1189 | b0928 | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | 0.903 |
| dadA | hisC | b1189 | b2021 | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | 0.903 |
| dadA | tyrB | b1189 | b4054 | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. | 0.902 |
| dadA | ybiC | b1189 | b0801 | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | Putative dehydrogenase; Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. | 0.900 |
| hisC | aspC | b2021 | b0928 | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | 0.956 |
| hisC | dadA | b2021 | b1189 | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | 0.903 |
| hisC | tyrB | b2021 | b4054 | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. | 0.958 |
| hisC | ybiB | b2021 | b0800 | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | Putative family 3 glycosyltransferase; Putative enzyme; Belongs to the anthranilate phosphoribosyltransferase family. | 0.598 |
| hisC | ybiC | b2021 | b0801 | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. | Putative dehydrogenase; Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. | 0.900 |
| rhaM | ybfB | b3901 | b0702 | L-rhamnose mutarotase; Involved in the anomeric conversion of L-rhamnose. | Putative membrane protein. | 0.893 |
| rhaM | ybiC | b3901 | b0801 | L-rhamnose mutarotase; Involved in the anomeric conversion of L-rhamnose. | Putative dehydrogenase; Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. | 0.531 |
| rhaM | yjaH | b3901 | b4001 | L-rhamnose mutarotase; Involved in the anomeric conversion of L-rhamnose. | DUF1481 family putative lipoprotein. | 0.544 |
| tyrB | aspC | b4054 | b0928 | Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. | 0.918 |
| tyrB | dadA | b4054 | b1189 | Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. | 0.902 |
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