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
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[Homology]
Score
pdxTGlutamine amidotransferase for pyridoxal phosphate synthesis; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (196 aa)    
Predicted Functional Partners:
pdxS
Glutamine amidotransferase for pyridoxal phosphate synthesis; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
 0.999
pdxK
Pyridoxine, pyridoxal, and pyridoxamine kinase; Phosphorylates B6 vitamers; functions in a salvage pathway. Uses pyridoxal, pyridoxine, and pyridoxamine as substrates. Can also use hydroxymethylpyrimidine (HMP) as substrate. Belongs to the ThiD family.
    
 0.976
guaA
GMP synthetase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.884
ywjH
Putative transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Does not show fructose-6-P aldolase activity.
  
 
  0.833
rbsK
Ribokinase; Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
     
 0.814
prs
Phosphoribosylpyrophosphate synthetase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P).
   
 
  0.805
tkt
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
   
 
  0.801
pgcA
Alpha-phosphoglucomutase; Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since glucose-1-phosphate is the precursor of UDP-glucose, which serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required fo [...]
     
  0.800
drm
Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family.
     
  0.800
ywlF
Ribose 5-phosphate epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
     
  0.800
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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