STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
rutRDna-binding transcriptional dual regulator rutr; 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) (212 aa)    
Predicted Functional Partners:
Peroxyureidoacrylate/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
Putative dihydroxyacetone-specific pts enzymes: hpr, ei components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone
Transcriptional repressor for the nemra-gloa operon, quinone-, glyoxal-, and hocl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS) . Represses the transcription of the nemRA-gloA operon by binding to the NemR box . May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA . Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS . Involved in response to methylglyoxal
Laci family transcriptional regulator, purine nucleotide synthesis repressor; Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. In addition, it participates in the regulation or coregulation of genes involved in de novo pyrimidine nucleotide biosynthesis, salvage and uptake (pyrC, pyrD, carAB and codBA), and of several genes encoding enzymes necessary for nucleotide and polyamine biosynthesis (prsA, glyA, gcvTHP, speA, glnB). Binds to a 16-bp palindromic sequence locat [...]
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
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
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
Deacetylase of acs and chey, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes
Guanine deaminase; Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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