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 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:
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Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
ribFBifunctional riboflavin kinase/fmn adenylyltransferase; Riboflavin biosynthesis protein RibF; Putative regulator; Not classified (313 aa)    
Predicted Functional Partners:
ribC
Riboflavin synthase, alpha subunit; Catalyzes the dismutation of two molecules of 6,7-dimethyl-8- ribityllumazine, resulting in the formation of riboflavin and 5-amino- 6-(D-ribitylamino)uracil
 
 0.993
ribD
Fused diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate
 
  
 0.973
yaaY
annotation not available
     
 0.971
ileS
Isoleucyl-trna synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile)
 
  
 0.966
ybjI
Fmn hydrolase / 5-amino-6-(5-phospho-d-ribitylamino)uracil phosphatase; Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D- ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway . Is also able to dephosphorylate flavin mononucleotide (FMN), erythrose 4-phosphate and other phosphoric acid esters
  
 0.923
yigB
Fmn hydrolase / 5-amino-6-(5-phospho-d-ribitylamino)uracil phosphatase; Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D- ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway . Is also able to dephosphorylate flavin mononucleotide (FMN) and other phosphoric acid esters . YigB is important for the formation of dormant persister cells
  
 
 0.922
ssuE
Nad(p)h-dependent fmn reductase; Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin
  
 
 0.909
fre
Nad(p)h-flavin reductase; Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides
  
 
  0.906
appA
Periplasmic AppA protein; Phosphoanhydride phosphorylase; pH 2.5 acid phosphatase; periplasmic; Protein involved in phosphorus metabolic process and response to starvation
     
  0.900
aphA
Acid phosphatase/phosphotransferase, class b, non-specific; Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6- phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. Also has a ph [...]
     
  0.900
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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