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 |
| apaH | rutD | b0049 | b1009 | Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | 0.617 |
| rutA | rutB | b1012 | b1011 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | Ureidoacrylate amidohydrolase; 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. | 0.999 |
| rutA | rutC | b1012 | b1010 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | 0.991 |
| rutA | rutD | b1012 | b1009 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | 0.985 |
| rutA | rutE | b1012 | b1008 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | Putative malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation; Belongs to the nitroreductase family. HadB/RutE subfamily. | 0.992 |
| rutA | rutF | b1012 | b1007 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | flavin:NADH reductase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin reductase Fre can substitute for the function of RutF, however, RutF is required for uracil utilization in vivo. | 0.999 |
| rutA | rutG | b1012 | b1006 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | Pyrimidine permease; May function as a proton-driven pyrimidine uptake system. | 0.937 |
| rutA | rutR | b1012 | b1013 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | Rut operon transcriptional repressor for; Master transcription regulator which represses the degradation of pyrimidines (rutABCDEFG) and purines (gcl operon) for maintenance of metabolic balance between pyrimidines and purines. It also regulates the synthesis of pyrimidine nucleotides and arginine from glutamine (carAB) and the supply of glutamate (gadABWX). | 0.645 |
| rutA | ydfG | b1012 | b1539 | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...] | 0.550 |
| rutB | rutA | b1011 | b1012 | Ureidoacrylate amidohydrolase; 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. | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | 0.999 |
| rutB | rutC | b1011 | b1010 | Ureidoacrylate amidohydrolase; 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. | Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | 0.999 |
| rutB | rutD | b1011 | b1009 | Ureidoacrylate amidohydrolase; 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. | Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | 0.999 |
| rutB | rutE | b1011 | b1008 | Ureidoacrylate amidohydrolase; 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. | Putative malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation; Belongs to the nitroreductase family. HadB/RutE subfamily. | 0.997 |
| rutB | rutF | b1011 | b1007 | Ureidoacrylate amidohydrolase; 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. | flavin:NADH reductase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin reductase Fre can substitute for the function of RutF, however, RutF is required for uracil utilization in vivo. | 0.999 |
| rutB | rutG | b1011 | b1006 | Ureidoacrylate amidohydrolase; 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. | Pyrimidine permease; May function as a proton-driven pyrimidine uptake system. | 0.983 |
| rutB | rutR | b1011 | b1013 | Ureidoacrylate amidohydrolase; 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. | Rut operon transcriptional repressor for; Master transcription regulator which represses the degradation of pyrimidines (rutABCDEFG) and purines (gcl operon) for maintenance of metabolic balance between pyrimidines and purines. It also regulates the synthesis of pyrimidine nucleotides and arginine from glutamine (carAB) and the supply of glutamate (gadABWX). | 0.810 |
| rutB | ydfG | b1011 | b1539 | Ureidoacrylate amidohydrolase; 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. | NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...] | 0.812 |
| rutC | rutA | b1010 | b1012 | Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | Pyrimidine oxygenase, FMN-dependent; 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. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. | 0.991 |
| rutC | rutB | b1010 | b1011 | Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | Ureidoacrylate amidohydrolase; 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. | 0.999 |
| rutC | rutD | b1010 | b1009 | Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. | 0.999 |
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