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Mettu_2038 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2038" - dITP/XTP pyrophosphatase in Methylobacter tundripaludum
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Predicted Interactions
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textmining
co-expression
protein homology
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Mettu_2038dITP/XTP pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions; Belongs to the HAM1 NTPase family (203 aa)    
Predicted Functional Partners:
rph
Ribonuclease PH; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (345 aa)
 
 
    0.993
guaB
Inosine-5’-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth; Belongs to the IMPDH/GMPR family (488 aa)
   
  0.974
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (528 aa)
 
 
  0.947
murI
Glutamate racemase; Provides the (R)-glutamate required for cell wall biosynthesis (270 aa)
 
    0.873
purA
Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family (430 aa)
   
  0.856
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (143 aa)
   
  0.852
Mettu_1685
Pyridoxal phosphate homeostasis protein; Pyridoxal 5’-phosphate (PLP)-binding protein, which is involved in PLP homeostasis (227 aa)
 
   
  0.843
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2’-deoxyuridine- 5’-monophosphate (dUMP) to 2’-deoxythymidine-5’-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis (277 aa)
   
 
  0.841
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)
   
 
  0.817
surE
5’-nucleotidase SurE; Nucleotidase that shows phosphatase activity on nucleoside 5’-monophosphates; Belongs to the SurE nucleotidase family (251 aa)
   
 
  0.798
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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