STRINGSTRING
STRING protein interaction network
Nodes:
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:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ugdUDP-glucose 6-dehydrogenase; Protein involved in cell surface antigen activity, host-interacting, colanic acid biosynthetic process and response to desiccation. (388 aa)    
Predicted Functional Partners:
wcaN
Putative regulatory subunit for GalU; Protein involved in nucleotide-sugar biosynthetic process.
  
 0.994
arnA
Fused UDP-L-Ara4N formyltransferase/UDP-GlcA C-4'-decarboxylase; Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides; In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily.
 
 0.987
galU
Glucose-1-phosphate uridylyltransferase; May play a role in stationary phase survival; Belongs to the UDPGP type 2 family.
  
 0.983
galE
UDP-galactose-4-epimerase; Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose.
  
 
 0.963
rfbC
dTDP-4-deoxyrhamnose-3,5-epimerase; Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
  
  
 0.962
glf
UDP-galactopyranose mutase, FAD/NAD(P)-binding; Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF); Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase family.
  
  
 0.925
wzxC
Putative colanic acid exporter; Probable export protein; Belongs to the polysaccharide synthase family.
 
  
 0.919
arnC
Undecaprenyl phosphate-L-Ara4FN transferase; Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides; Belongs to the glycosyltransferase 2 family.
  
  
 0.915
wzxB
Putative polisoprenol-linked O-antigen transporter; May be involved in the translocation process of the nascent O-polysaccharide molecules and/or its ligation to lipid A core units.
  
  
 0.914
rfbA
Glucose-1-phosphate thymidylyltransferase; Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Belongs to the glucose-1-phosphate thymidylyltransferase family.
  
  
 0.904
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.