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purE protein (Methanococcus voltae) - STRING interaction network
"purE" - N5-carboxyaminoimidazole ribonucleotide mutase in Methanococcus voltae
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second shell of interactors
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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purEN5-carboxyaminoimidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (156 aa)    
Predicted Functional Partners:
purC
TIGRFAM- phosphoribosylaminoimidazole-succinocarboxamide synthase; KEGG- nam-NAMH_0651 phosphoribosylaminoimidazole-succinocarboxamide synthase; PFAM- SAICAR synthetase (244 aa)
 
  0.997
purD
TIGRFAM- phosphoribosylamine/glycine ligase; KEGG- sat-SYN_02439 phosphoribosylamine--glycine ligase; PFAM- Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase, N-domain; Phosphoribosylglycinamide synthetase, C-domain; Belongs to the GARS family (445 aa)
   
  0.993
purM
KEGG- hypothetical protein; K01933 phosphoribosylformylglycinamidine cyclo-ligase; TIGRFAM- phosphoribosylformylglycinamidine cyclo-ligase; PFAM- AIR synthase related protein domain protein; AIR synthase related protein (352 aa)
 
   
  0.961
purT
Formate-dependent phosphoribosylglycinamide formyltransferase; Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate; Belongs to the PurK/PurT family (395 aa)
 
   
  0.955
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine (462 aa)
 
   
  0.949
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 [...] (740 aa)
 
   
  0.901
Mvol_1664
KEGG- sfu-Sfum_0660 adenylosuccinate lyase; TIGRFAM- adenylosuccinate lyase; PFAM- fumarate lyase; Adenylosuccinate lyase-like; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily (448 aa)
   
   
  0.854
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 [...] (225 aa)
 
   
  0.838
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8- ribityllumazine by condensation of 5-amino-6-(D- ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family (138 aa)
   
   
  0.755
purS
Phosphoribosylformylglycinamidine synthase subunit PurS; 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 [...] (82 aa)
         
  0.724
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3
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