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dtd protein (Methylobacter tundripaludum) - STRING interaction network
"dtd" - D-aminoacyl-tRNA deacylase in Methylobacter tundripaludum
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Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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dtdD-aminoacyl-tRNA deacylase ; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo (148 aa)    
Predicted Functional Partners:
Mettu_0039
AIG2 family protein (134 aa)
              0.859
lpxH
UDP-2,3-diacylglucosamine diphosphatase ; Catalyzes the hydrolysis of the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1- phosphate (lipid X) and UMP (241 aa)
   
   
  0.642
hisS
Histidyl-tRNA synthetase (424 aa)
   
      0.596
Mettu_2188
RelA/SpoT family protein ; In eubacteria ppGpp (guanosine 3’-diphosphate 5-’ diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance (710 aa)
 
     
  0.596
lpxK
Lipid A 4’-kinase ; Transfers the gamma-phosphate of ATP to the 4’-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1- P) to form tetraacyldisaccharide 1,4’-bis-phosphate (lipid IVA) (333 aa)
           
  0.561
Mettu_1763
GTP-binding protein TypA (603 aa)
 
          0.554
tyrS
Tyrosyl-tRNA synthetase ; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (398 aa)
   
   
  0.552
Mettu_2548
(P)ppGpp synthetase I, SpoT/RelA ; In eubacteria ppGpp (guanosine 3’-diphosphate 5-’ diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance (723 aa)
         
  0.538
pfp
Pyrophosphate-dependent 6-phosphofructose-1-kinase ; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions (409 aa)
              0.520
Mettu_2827
3-phosphoshikimate 1-carboxyvinyltransferase ; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate (733 aa)
   
        0.518
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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