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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
yutFPutative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro; Belongs to the HAD-like hydrolase superfamily. NagD family. (256 aa)    
Predicted Functional Partners:
yutE
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the UPF0331 family.
  
  
 0.977
yutD
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12770717.
 
  
 0.948
ysaA
Putative phosphatase; 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; Belongs to the HAD-like hydrolase superfamily.
   
  
 0.853
ycsE
Putative 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.
      
 0.850
ywhB
1,3-keto-enol tautomerase; Catalyzes both 1,3- and 1,5-keto-enol tautomerization of the diacid 2-hydroxymuconate (2-hydroxy-2,4-hexadienedioate) to produce 2- oxo-4-hexenedioate. This reaction is highly stereoselective and produces a mixture of stereoisomers, where the (3S)-isomer of 2-oxo-4- hexenedioate predominates. Also catalyzes the tautomerization of 2- hydroxymuconate to 2-oxo-3-hexenedioate, however this reaction is slower and occurs after the tautomerization of 2-hydroxymuconate to 2- oxo-4-hexenedioate. Using 2-hydroxy-2,4-pentadienoate, phenylenolpyruvate, (p-hydroxyphenyl)- [...]
   
  
 0.758
yitU
Putative phosphatase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro.
   
  
 0.756
yqeG
Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
      
 0.750
suhB
Inositol monophosphatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the inositol monophosphatase superfamily.
 
   
 0.749
ppaX
P-Ser-HPr phosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool; Belongs to the HAD-like hydrolase superfamily. PpaX family.
   
  
 0.742
ywtE
Putative hydrolase; 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.
   
  
 0.692
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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