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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
pssAPhosphatidylserine synthase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. (177 aa)    
Predicted Functional Partners:
psd
Phosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer); Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
 
 
 0.999
cdsA
Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 
 0.955
pgsA
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase; This protein catalyzes the committed step to the synthesis of the acidic phospholipids; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
 
 
 0.955
ybfM
Putative membrane phosphatase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
  
 0.920
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.
    
  0.903
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity).
    
  0.902
sdaAB
L-serine dehydratase (beta chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
  0.900
sdaAA
L-serine dehydratase (alpha chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
  0.900
trpA
Tryptophan synthase (alpha subunit); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate; Belongs to the TrpA family.
     
  0.900
trpB
Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.900
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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