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
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Textmining
[Homology]
Score
purLPhosphoribosylformylglycinamidine synthase; 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 [...] (963 aa)    
Predicted Functional Partners:
KPK78193.1
Phosphoribosylformylglycinamidine synthase; 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 [...]
 0.999
KPK72288.1
Amidophosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.995
KPK75644.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.986
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase; Involved in de novo purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.982
KPK77175.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.979
purC
Phosphoribosylaminoimidazole-succinocarboxamide synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SAICAR synthetase family.
 
 0.973
KPK77211.1
Adenylosuccinate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
  
  
 0.924
KPK75915.1
Glycine cleavage system protein T; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.924
purA
Hypothetical protein; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.
  
  
 0.907
fhs
Formate--tetrahydrofolate ligase; Catalyzes the formation of 10-formyltetrahydrofolate from formate and tetrahydrofolate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the formate--tetrahydrofolate ligase family.
  
 
 0.898
Your Current Organism:
Phycisphaerae bacterium SM2330
NCBI taxonomy Id: 1703411
Other names: P. bacterium SM23_30, Phycisphaerae bacterium SM23_30
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