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
yigB5-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. Belongs to the HAD-like hydrolase superfamily. (238 aa)    
Predicted Functional Partners:
ybjI
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. Belongs to the HAD-like hydrolase superfamily. Cof family.
     
 0.980
ribD
Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
    
 0.947
ribF
Bifunctional riboflavin kinase/FAD synthetase; Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD; Belongs to the RibF family.
  
 
 0.915
ribE
Riboflavin synthase beta chain; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
     
 0.915
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.
   
 
 0.913
ssuE
NAD(P)H-dependent FMN reductase; Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
  
 
  0.901
fre
NAD(P)H-flavin reductase; Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides; Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family.
  
 
  0.901
appA
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
xerC
Site-specific tyrosine recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or [...]
  
    0.870
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
Server load: low (26%) [HD]