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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ycsE5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro . To a lesser extent, may also catalyze the dephosphorylation of a broad range of substrates such as phosphorylated sugars and triphosphate nucleotides in vitro (249 aa)    
Predicted Functional Partners:
ribH
6,7-dimethyl-8-ribityllumazine synthase, beta subunit; 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. Is able to use the non-natural R enantiomer of 3,4- dihydroxy-2-butanone 4-phosphate as a substrate, but with less efficiency than the natural S enantiomer. Cannot use unphosphorylated 3,4-dihydroxy-2-butanone, 3,4-dihydroxy-2-butanone 3-phosphate or diacetyl as substrates
    
 0.957
ribD
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
    
 0.940
yutF
Putative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro
   
  
 0.909
ribE
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
     
  0.900
yitU
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro
 
  
0.889
ysaA
Putative hydrolase of the had superfamily; Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro
      
 0.886
yqeM
Conserved hypothetical protein; May be a S-adenosyl-L-methionine (SAM)-dependent methyltransferase
   
  
 0.882
ywtE
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro . Also catalyzes the dephosphorylation of phosphorylated 5-6 carbon sugars and monophosphate nucleotides (NMP) in vitro
  
  
0.876
suhB
Myo-inositol-1(or 4)-monophosphatase; Belongs to the inositol monophosphatase superfamily
  
  
 0.871
yqeG
Uncharacterized protein YqeG; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme
      
 0.710
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (6%) [HD]