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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AOE41367.1 | rutB_2 | BEE12_16815 | BEE12_13790 | Monooxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.517 |
| gatA_4 | rutB_2 | BEE12_10010 | BEE12_13790 | Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.733 |
| nadR_2 | rutB_2 | BEE12_09930 | BEE12_13790 | Trifunctional NAD biosynthesis/regulator protein NadR; Catalyzes the formation of NAD(+) from nicotinamide ribonucleotide; catalyzes the formation of nicotinamide mononucleotide from nicotinamide riboside; also has a regulatory function; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.443 |
| rutA_1 | rutB_2 | BEE12_13795 | BEE12_13790 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.995 |
| rutA_1 | rutC_2 | BEE12_13795 | BEE12_13785 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.929 |
| rutA_1 | rutD | BEE12_13795 | BEE12_13780 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | Pyrimidine utilization protein D; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family. | 0.957 |
| rutA_1 | rutE | BEE12_13795 | BEE12_07050 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | Malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. | 0.734 |
| rutA_1 | rutF | BEE12_13795 | BEE12_13775 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | Pyrimidine utilization flavin reductase protein F; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway; Belongs to the non-flavoprotein flavin reductase family. RutF subfamily. | 0.991 |
| rutA_1 | rutG | BEE12_13795 | BEE12_13770 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | Pyrimidine utilization transport protein G; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.655 |
| rutA_1 | rutR_2 | BEE12_13795 | BEE12_13800 | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | TetR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.582 |
| rutB_2 | AOE41367.1 | BEE12_13790 | BEE12_16815 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Monooxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.517 |
| rutB_2 | gatA_4 | BEE12_13790 | BEE12_10010 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.733 |
| rutB_2 | nadR_2 | BEE12_13790 | BEE12_09930 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Trifunctional NAD biosynthesis/regulator protein NadR; Catalyzes the formation of NAD(+) from nicotinamide ribonucleotide; catalyzes the formation of nicotinamide mononucleotide from nicotinamide riboside; also has a regulatory function; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.443 |
| rutB_2 | rutA_1 | BEE12_13790 | BEE12_13795 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | 0.995 |
| rutB_2 | rutC_2 | BEE12_13790 | BEE12_13785 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.988 |
| rutB_2 | rutD | BEE12_13790 | BEE12_13780 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Pyrimidine utilization protein D; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family. | 0.993 |
| rutB_2 | rutE | BEE12_13790 | BEE12_07050 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. | 0.431 |
| rutB_2 | rutF | BEE12_13790 | BEE12_13775 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Pyrimidine utilization flavin reductase protein F; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway; Belongs to the non-flavoprotein flavin reductase family. RutF subfamily. | 0.983 |
| rutB_2 | rutG | BEE12_13790 | BEE12_13770 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | Pyrimidine utilization transport protein G; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.572 |
| rutB_2 | rutR_2 | BEE12_13790 | BEE12_13800 | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | TetR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.520 |
page 1 of 3