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
purSHypothetical 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 to assist in the transfer of the am [...] (86 aa)    
Predicted Functional Partners:
purC
Phosphoribosylaminoimidazolesuccinocarboxamide (SAICAR) synthase; Belongs to the SAICAR synthetase family.
  
  
 0.999
purQ
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain; 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 [...]
 
 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.
  
 0.999
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.
  
 
 0.999
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
 
 0.998
purE
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
  
 
 0.997
purD
Phosphoribosylamine--glycine ligase; Belongs to the GARS family.
  
 0.996
purH
AICAR transformylase IMP cyclohydrolase PurH.
  
 
 0.995
purK
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase); Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
 
  
 0.969
Your Current Organism:
Lactobacillus camelliae
NCBI taxonomy Id: 1423730
Other names: L. camelliae DSM 22697 = JCM 13995, Lactobacillus camelliae DSM 22697, Lactobacillus camelliae DSM 22697 = JCM 13995, Lactobacillus camelliae JCM 13995, Lactobacillus camelliae JCM 13995 = DSM 22697
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