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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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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.
  
  
 0.980
yutD
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12770717.
 
  
 0.949
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.
   
  
 0.902
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.
   
  
 0.880
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.
   
  
 0.839
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.
   
  
 0.768
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)- [...]
   
  
 0.741
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.
      
 0.695
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.
 
  
 0.678
yfkN
Exported 2',3'-cyclic-nucleotide 2'-phosphodiesterase, 2' (or 3') nucleotidase and 5' nucleotidase; Catalyzes the release of inorganic phosphate from 2',3'- cyclic nucleotides through consecutive 2',3'-phosphodiesterase and 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase activity. Does not catalyze the release of inorganic phosphate from 3',5'-cyclic nucleotides. Probably plays a role in the cellular reprocessing of nucleotides present in the medium, under conditions of phosphate shortage.
  
  
 0.670
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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