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
glmUFused N-acetyl glucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyl transferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. (456 aa)    
Predicted Functional Partners:
glmM
Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate.
 
 0.999
glmS
L-glutamine:D-fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
  
 0.998
murA
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic fosfomycin; Belongs to the EPSP synthase family. MurA subfamily.
 
 
 0.989
prs
Phosphoribosylpyrophosphate synthase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P).
  
 0.982
wecB
UDP-N-acetyl glucosamine-2-epimerase; Catalyzes the reversible epimerization at C-2 of UDP-N- acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP- N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption.
  
 
 0.954
murC
UDP-N-acetylmuramate:L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
   
 0.948
lpxA
UDP-N-acetylglucosamine acetyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
  
 
 0.896
murE
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso- diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine.
 
  
 0.894
pta
Phosphate acetyltransferase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. In the N-terminal section; belongs to the CobB/CobQ family.
  
 
 0.882
atpE
F0 sector of membrane-bound ATP synthase, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
 
  
 0.853
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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