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
Databases
Textmining
[Homology]
Score
purFAmidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (508 aa)    
Predicted Functional Partners:
purD
Phosphoribosylamine--glycine ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GARS family.
 0.999
purM
Phosphoribosylformylglycinamidine cyclo-ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
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 [...]
 
 
 0.997
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 [...]
 
 0.997
purE
5-(carboxyamino)imidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
  
 0.992
carB
Carbamoyl phosphate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CarB family.
 
 
 0.986
purH
Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.982
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.
 
 
 0.978
carA
Carbamoyl phosphate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CarA family.
 
 
 0.977
purK
5-(carboxyamino)imidazole ribonucleotide synthase; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
 
  
 0.977
Your Current Organism:
Mycobacterium chimaera
NCBI taxonomy Id: 222805
Other names: CCUG 50989, CIP 107892, DSM 44623, JCM 14737, M. chimaera, Mycobacterium chimaera Tortoli et al. 2004, NCTC 13781, personal::FI-01069, strain FI-01069
Server load: low (30%) [HD]