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
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[Homology]
Score
purSPhosphoribosylformylglycinamidine synthase, purS protein; 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 [...] (84 aa)    
Predicted Functional Partners:
purQ
Phosphoribosylformylglycinamidine synthase 1; 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
purL
Phosphoribosylformylglycinamidine synthase 2; 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
purM
Phosphoribosylformylglycinamidine cyclo-ligase.
  
 0.998
purN
Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
 
 
 0.998
purC
Phosphoribosylaminoimidazolesuccinocarboxamide synthase; Belongs to the SAICAR synthetase family.
 
  
 0.990
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
 
  
 0.990
purH
Bifunctional purine biosynthesis protein PurH.
  
  
 0.985
purD
Phosphoribosylamine-glycine ligase; Belongs to the GARS family.
  
 
 0.984
purE
N5-carboxyaminoimidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
  
  
 0.900
purK
Phosphoribosylaminoimidazole carboxylase, ATPase subunit; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
  
  
 0.886
Your Current Organism:
Enterococcus mundtii
NCBI taxonomy Id: 53346
Other names: ATCC 43186, CCUG 18656, CFBP 4251, CIP 103010, DSM 4838, E. mundtii, Enterobacter sp. PX-E.sp.Jor, JCM 8731, LMG 10748, LMG:10748, MUTK 559, NBRC 100490, NCDO 2375, NCIMB 702375, NCTC 12363
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