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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Experiments
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[Homology]
Score
ACI18355.1Phosphoribosylformylglycinamidine cyclo-ligase. (62 aa)    
Predicted Functional Partners:
purS
Phosphoribosylformylglycinamidine 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 [...]
  
 0.968
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 [...]
  
 
 0.965
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 [...]
  
 
 0.965
ACI18843.1
Phosphoribosylformylglycinamidine cyclo-ligase.
    
  0.956
ACI18515.1
Phosphoribosylformylglycinamidine cyclo-ligase; Identified by match to protein family HMM PF02769.
    
  0.956
purM
Phosphoribosylformylglycinamidine cyclo-ligase; Identified by match to protein family HMM PF00586; match to protein family HMM PF02769; match to protein family HMM TIGR00878.
     
  0.900
ACI18831.1
ThiC family; Identified by match to protein family HMM PF01964.
     
 0.802
ACI19678.1
Hypothetical protein; Identified by glimmer; putative.
       0.773
purB
Adenylosuccinate lyase; Identified by match to protein family HMM PF00206; match to protein family HMM TIGR00928; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
  
 
 0.694
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
  
  
 0.680
Your Current Organism:
Dictyoglomus thermophilum
NCBI taxonomy Id: 309799
Other names: D. thermophilum H-6-12, Dictyoglomus thermophilum H-6-12
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