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:
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[Homology]
Score
purKPhosphoribosylaminoimidazole carboxylase ATPase subunit EC 41121; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (368 aa)    
Predicted Functional Partners:
purE
Phosphoribosylaminoimidazole carboxylase catalytic subunit EC 41121; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
 0.999
purM
Phosphoribosylformylglycinamidine cycloligase EC 6331.
 
 
 0.998
purQ
Phosphoribosylformylglycinamidine synthase glutamine amidotransferase subunit EC 6353; 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 [...]
 
 
 0.969
purL
Phosphoribosylformylglycinamidine synthase synthetase subunit EC 6353; 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 a [...]
 
 
 0.969
purC-2
Phosphoribosylaminoimidazolesuccinocarboxamide synthase EC 6326; Belongs to the SAICAR synthetase family.
 
 
 0.966
purS
Phosphoribosylformylglycinamidine synthase PurS subunit EC 6353; 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 [...]
 
 
 0.953
purH
IMP cyclohydrolase EC 35410 Phosphoribosylaminoimidazolecarboxamide formyltransferase EC 2123.
 
  
 0.948
purD
Phosphoribosylamineglycine ligase EC 63413; Belongs to the GARS family.
 
 
 0.946
purF
Amidophosphoribosyltransferase EC 24214; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
 
  
 0.937
purC
Phosphoribosylaminoimidazolesuccinocarboxamide synthase EC 6326; Belongs to the SAICAR synthetase family.
  
 
 0.918
Your Current Organism:
Bradyrhizobium sp.
NCBI taxonomy Id: 376
Other names: B. sp.
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