STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
purFAmidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (459 aa)    
Predicted Functional Partners:
purQ
Phosphoribosylformylglycinamidine synthase I; 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 to assist i [...]
 
 
 0.999
purE
Phosphoribosylaminoimidazole carboxylase catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
  
 0.999
purD
Phosphoribosylamine--glycine ligase; Citation: Kanai S, Toh H. (1999) J Mol Evol 48:482-92.
 0.999
purB
Adenylosuccinate lyase; Citation: Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO. (2000) J Mol Biol 301:433-50; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
 
 
 0.999
purM-2
AIR synthase related protein:Phosphoribosylformylglycinamidine cyclo-ligase.
  
 0.999
purL
Phosphoribosylformylglycinamidine synthase II; 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 to assist [...]
 
 0.998
purC
Phosphoribosylaminoimidazole-succinocarboxamide synthase; Citation: Tiedeman AA, DeMarini DJ, Parker J, Smith JM. (1990) J Bacteriol 172:6035-41; Belongs to the SAICAR synthetase family.
 
 
 0.997
carB
Carbamoyl-phosphate synthase large chain; Citation: Nicoloff H, Hubert JC, Bringel F. (2000). J. Bacteriol. 182:3416-3422; Belongs to the CarB family.
  
 
 0.990
carA
Carbamoyl-phosphate synthase small chain; Citation: Nicoloff H, Hubert JC, Bringel F. (2000). J. Bacteriol. 182:3416-3422; Belongs to the CarA family.
  
 
 0.979
prsA
Phosphoribosyltransferase:Purine/pyrimidine phosphoribosyl transferase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P).
  
 0.965
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.