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 |
| hyuA | preA | b2873 | b2147 | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | Dihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). | 0.994 |
| hyuA | ygeW | b2873 | b2870 | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | 0.922 |
| hyuA | ygeX | b2873 | b2871 | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | 0.921 |
| hyuA | ygeY | b2873 | b2872 | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | Putative deacetylase. | 0.960 |
| preA | hyuA | b2147 | b2873 | Dihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | 0.994 |
| preA | ygeW | b2147 | b2870 | Dihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | 0.542 |
| preA | ygeY | b2147 | b2872 | Dihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). | Putative deacetylase. | 0.689 |
| ygeW | hyuA | b2870 | b2873 | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | 0.922 |
| ygeW | preA | b2870 | b2147 | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | Dihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). | 0.542 |
| ygeW | ygeX | b2870 | b2871 | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | 0.967 |
| ygeW | ygeY | b2870 | b2872 | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | Putative deacetylase. | 0.992 |
| ygeX | hyuA | b2871 | b2873 | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | 0.921 |
| ygeX | ygeW | b2871 | b2870 | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | 0.967 |
| ygeX | ygeY | b2871 | b2872 | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | Putative deacetylase. | 0.996 |
| ygeY | hyuA | b2872 | b2873 | Putative deacetylase. | D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. | 0.960 |
| ygeY | preA | b2872 | b2147 | Putative deacetylase. | Dihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). | 0.689 |
| ygeY | ygeW | b2872 | b2870 | Putative deacetylase. | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. | 0.992 |
| ygeY | ygeX | b2872 | b2871 | Putative deacetylase. | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | 0.996 |