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dtd protein (Methylobacter tundripaludum) - STRING interaction network
"dtd" - D-aminoacyl-tRNA deacylase in Methylobacter tundripaludum
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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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dtdD-aminoacyl-tRNA deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl- tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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 and helps enforce protein L-homochirality; Belongs to the DTD family (148 aa)    
Predicted Functional Partners:
Mettu_0039
AIG2 family protein; PFAM- AIG2-like; KEGG- bja-bll7352 hypothetical protein (134 aa)
              0.848
cca
Multifunctional CCA protein; Catalyzes the addition and repair of the essential 3’- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2’- nucleotidase and 2’,3’-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3’-CCA terminus degraded by intracellular RNases (407 aa)
     
      0.539
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (543 aa)
     
 
    0.512
Mettu_3580
Probable S-methyl-5’-thioinosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5’- thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1- phosphate. Involved in the breakdown of S-methyl-5’-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine (242 aa)
       
    0.509
lpxH
UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (241 aa)
         
  0.503
pfp
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase; 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)
              0.494
Mettu_3548
KEGG- mca-MCA1224 thioesterase family protein; TIGRFAM- Tol-Pal system-associated acyl-CoA thioesterase; 4-hydroxybenzoyl-CoA thioesterase; PFAM- Thioesterase superfamily (134 aa)
           
  0.480
Mettu_3455
PFAM- Metallophosphoesterase; KEGG- mag-amb0266 hypothetical protein (262 aa)
         
  0.464
Mettu_1493
PFAM- Glyoxalase/bleomycin resistance protein/dioxygenase; KEGG- mes-Meso_1734 glyoxalase/bleomycin resistance protein/dioxygenase (146 aa)
         
  0.463
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...] (371 aa)
 
   
  0.450
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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