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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ylbEannotation not available (419 aa)    
Predicted Functional Partners:
fdrA
Protein FdrA; Not known; multicopy suppressor of dominant negative ftsH mutations
  
 0.995
ylbF
Uncharacterized protein YlbF; Putative carboxylase
 
  
 0.987
nuoC
NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family
   
  
 0.976
yahF
Uncharacterized protein YahF; Putative oxidoreductase subunit; To E.coli FdrA and some, to bacterial SucD
    0.956
ybcF
Putative carbamate kinase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process
 
   
 0.925
allD
Ureidoglycolate dehydrogenase (NAD(+)); AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate
 
     0.834
allE
(S)-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S- ureidoglycine; Belongs to the UGHY family
 
     0.812
pfo
Probable pyruvate-flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin
  
  
 0.775
yhhZ
annotation not available
      
 0.741
allC
Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S- ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen
 
     0.692
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 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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