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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
purFAmidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (462 aa)    
Predicted Functional Partners:
carB
Carbamoyl-phosphate synthase, large subunit; Identified by similarity to SP:P00968; match to protein family HMM PF00289; match to protein family HMM PF02142; match to protein family HMM PF02786; match to protein family HMM PF02787; match to protein family HMM TIGR01369.
 
 0.999
purD
Phosphoribosylamine--glycine ligase; Identified by similarity to SP:P15640; match to protein family HMM PF01071; match to protein family HMM PF02842; match to protein family HMM PF02843; match to protein family HMM PF02844; match to protein family HMM TIGR00877; Belongs to the GARS family.
 0.999
purM
Phosphoribosylformylglycinamidine cyclo-ligase; Identified by similarity to SP:P08178; match to protein family HMM PF00586; match to protein family HMM PF02769; match to protein family HMM TIGR00878.
  
 0.999
purQ
Phosphoribosylformylglycinamidine synthase I.
 
 
 0.997
purB
Adenylosuccinate lyase; Identified by similarity to SP:P12047; match to protein family HMM PF00206; match to protein family HMM TIGR00928; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
 
 
 0.992
DVU_3235
IMP cyclohydrolase, putative; Identified by similarity to SP:P12048; match to protein family HMM PF02142.
 
 
 0.988
DVU_3206
Phosphoribosylaminoimidazolecarboxamide formyltransferase, putative; Identified by similarity to SP:P12048; match to protein family HMM PF01808.
 
 
 0.987
purE
Phosphoribosylaminoimidazole carboxylase, catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
  
 0.986
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.
 
 
 0.984
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 [...]
 
 0.983
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.