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fmt protein (Escherichia coli K12 DH10B) - STRING interaction network
"fmt" - methionyl-tRNA formyltransferase in Escherichia coli K12 DH10B
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Predicted Interactions
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textmining
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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 (315 aa)    
Predicted Functional Partners:
def
Peptide 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 (169 aa)
 
  0.997
sun
16S rRNA methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA (429 aa)
   
   
  0.888
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 (677 aa)
   
 
  0.884
folD
Bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate. This enzyme is specific for NADP (288 aa)
   
 
  0.855
smf
DNA protecting protein DprA (374 aa)
 
     
  0.789
priA
Primosome assembly protein PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Is also involved in initiation of normal DNA replication in various plasmids and phages. Binds to branched DNA structures that resemble D-loops or to the primosome assembly site (PAS). Binds to DNA in two distinct modes, either dependent on or independent of the 3’ ter [...] (732 aa)
 
   
  0.782
metH
B12-dependent methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (1227 aa)
     
 
  0.763
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. Thus, is able to catalyze the cleavage of allothreonine and 3- phenylserine. Also catalyzes the irreversible conversion of 5,10 [...] (417 aa)
     
 
  0.750
pheT
phenylalanyl-tRNA synthetase subunit beta (795 aa)
 
 
  0.736
aroE
Shikimate 5-dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD (272 aa)
   
   
  0.727
Your Current Organism:
Escherichia coli K12 DH10B
NCBI taxonomy Id: 316385
Other names: E. coli str. K-12 substr. DH10B, Escherichia coli DH10B, Escherichia coli K12 DH10B, Escherichia coli str. K-12 substr. DH10B, Escherichia coli str. K12 substr. DH10B, Escherichia coli strain K12 substrain DH10B
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