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
ywhB1,3-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)- [...] (62 aa)    
Predicted Functional Partners:
catE
Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
    
 0.919
yutF
Putative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro; Belongs to the HAD-like hydrolase superfamily. NagD family.
   
  
 0.758
yodD
Putative hydrolase; Putative hydrolase that may contribute to the degradation of aromatic compounds.
      
 0.688
yrhG
Putative formate/nitrite transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
      
 0.682
pucR
Transcriptional regulator of the purine degradation operon; Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression. Belongs to the CdaR family.
      
 0.680
yszB
Conserved hypothetical protein containing an ACT domain; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 2537815; Belongs to the UPF0735 family.
  
   
 0.627
ywhD
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
    0.605
ywhC
Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the peptidase M50B family.
       0.603
yfmT
Putative aldehyde dehydrogenase; A benzaldehyde dehydrogenase able to act on substrates with 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4- hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro. The physiological substrate is unknown.
     
 0.578
bsdC
Phenolic acid decarboxylase subunit BsdC; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4- hydroxybenzoate and vanillate. Could also catalyze the decarboxylation of salicylate (Probable). Is not active on di- and tri-hydroxybenzoate derivatives. Belongs to the UbiD family. YclC subfamily.
      
 0.565
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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