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STRINGSTRING
purM protein (Thermoproteus tenax) - STRING interaction network
"purM" - annotation not available in Thermoproteus tenax
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
purMannotation not available (307 aa)    
Predicted Functional Partners:
purD
annotation not available (485 aa)
 
  0.999
purN
annotation not available (277 aa)
   
  0.999
purQ
Phosphoribosylformylglycinamidine synthase subunit PurQ; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought t [...] (210 aa)
  0.999
purL
Phosphoribosylformylglycinamidine synthase subunit PurL; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought t [...] (700 aa)
 
  0.999
TTX_1960
annotation not available (417 aa)
   
  0.996
TTX_1969
N5-carboxyaminoimidazole ribonucleotide synthase; Catalyzes the ATP-dependent conversion of 5- aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5- carboxyaminoimidazole ribonucleotide (N5-CAIR); Belongs to the PurK/PurT family (366 aa)
 
 
  0.995
purE
N5-carboxyaminoimidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (152 aa)
 
   
  0.988
TTX_1961
annotation not available (371 aa)
   
  0.974
purC
annotation not available (233 aa)
 
   
  0.971
folD
Bifunctional protein FolD; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate (317 aa)
         
  0.904
Your Current Organism:
Thermoproteus tenax
NCBI taxonomy Id: 768679
Other names: T. tenax Kra 1, Thermoproteus tenax, Thermoproteus tenax DSM 2078, Thermoproteus tenax JCM 9277, Thermoproteus tenax Kra 1, Thermoproteus tenax str. Kra 1, Thermoproteus tenax strain Kra 1
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