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
pdxSConserved hypothetical protein; 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. Belongs to the PdxS/SNZ family. (297 aa)    
Predicted Functional Partners:
pdxT
Putative amidotransferase; 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.
 0.999
pdxY
Putative pyridoxamine kinase; Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
   
 0.910
lipB
Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
      
 0.869
rbsK
Putative 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.
     
 0.818
tal
Transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the transaldolase family. Type 2 subfamily.
    
  0.813
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.
   
 
  0.808
prsA
Ribose-phosphate pyrophosphokinase; 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); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
   
 
  0.803
DIP1796
Putative ribose/galactose isomerase; Similar to Staphylococcus aureus galactose-6-phosphate isomerase subunit LacB SW:LACB_STAAU (P26592) (171 aa) fasta scores: E(): 2e-13, 36.53% id in 156 aa, and to Mycobacterium tuberculosis putative isomerase Rv2465c TR:AAK46840 (EMBL:AL021246) (159 aa) fasta scores: E(): 4.1e-45, 76.77% id in 155 aa.
     
  0.800
pgm
Phosphoglucomutase; Similar to Escherichia coli phosphoglucomutase Pgm SW:PGMU_ECOLI (P36938) (546 aa) fasta scores: E(): 2.7e-133, 62.5% id in 544 aa, and to Mycobacterium tuberculosis hypothetical protein Rv3068c TR:P95090 (EMBL:Z83866) (547 aa) fasta scores: E(): 7e-150, 69.76% id in 549 aa.
     
  0.800
DIP0226
Similar to Streptomyces coelicolor putative GntR-family regulator SC5G8.04 TR:Q9KZB0 (EMBL:AL353872) (462 aa) fasta scores: E(): 8.4e-38, 36.46% id in 458 aa.
  
  
 0.768
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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