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purH protein (Methylobacter tundripaludum) - STRING interaction network
"purH" - Bifunctional purine biosynthesis protein PurH in Methylobacter tundripaludum
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
purHBifunctional purine biosynthesis protein PurH (535 aa)    
Predicted Functional Partners:
purD
Phosphoribosylglycinamide synthetase (426 aa)
  0.999
purM
Phosphoribosyl-aminoimidazole synthetase (347 aa)
 
  0.999
purL
Formylglycinamide ribonucleotide amidotransferase ; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (1289 aa)
   
   
  0.999
Mettu_0644
Adenylosuccinase (454 aa)
   
  0.999
purC
SAICAR synthetase (297 aa)
   
 
  0.999
purE
5-(carboxyamino)imidazole ribonucleotide mutase ; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (166 aa)
 
 
  0.998
purF
Glutamine phosphoribosylpyrophosphate amidotransferase ; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine (502 aa)
 
 
  0.996
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)
   
  0.994
purA
IMP--aspartate ligase ; 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 (430 aa)
 
  0.992
Mettu_1869
Inosine-5’-monophosphate dehydrogenase (488 aa)
   
  0.992
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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