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fmt protein (Methylobacter tundripaludum) - STRING interaction network
"fmt" - Methionyl-tRNA formyltransferase in Methylobacter tundripaludum
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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fmtMethionyl-tRNA formyltransferase ; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (309 aa)    
Predicted Functional Partners:
Mettu_3771
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (168 aa)
 
  0.997
Mettu_3769
Ribosomal RNA small subunit methyltransferase B (435 aa)
 
   
  0.963
metG
Methionyl-tRNA synthetase ; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (672 aa)
   
 
  0.952
Mettu_3766
Putative two component, sigma54 specific, transcriptional regulator (453 aa)
 
          0.916
glyA
Serine hydroxymethyltransferase ; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF- independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (417 aa)
     
 
  0.913
Mettu_3768
Putative uncharacterized protein (194 aa)
              0.912
Mettu_3767
Multi-sensor signal transduction histidine kinase (724 aa)
              0.912
Mettu_1997
Dihydrofolate reductase ; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (163 aa)
 
 
  0.908
Mettu_0638
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (178 aa)
 
  0.887
Mettu_1405
Methionine synthase (1226 aa)
     
 
  0.883
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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