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
purHPhosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Similar to SP:P15639 GB:J05126 GB:X51950 PID:147420 PID:396345; identified by sequence similarity; putative. (530 aa)    
Predicted Functional Partners:
purD
Phosphoribosylamine--glycine ligase; Similar to SP:P15640 GB:J05126 GB:X51950 PID:147421 PID:396344; identified by sequence similarity; putative.
 
 
 0.999
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
 
 
 0.999
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.
 0.999
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.
 
 0.997
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
  
  
 0.997
VC_1126
Adenylosuccinate lyase; Similar to GB:M74924 SP:P25739 PID:145203 PID:42585 GB:U00096; identified by sequence similarity; putative; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
  
 0.996
guaC
GMP reductase; Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
  
 0.994
purM
Phosphoribosylformylglycinamidine cyclo-ligase; Similar to GB:M13747 SP:P08178 PID:147425 GB:U00096 PID:1788845; identified by sequence similarity; putative.
 
  
 0.993
purA
Adenylosuccinate synthetase; 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.
  
 0.991
purC
Phosphoribosylaminoimidazole-succinocarboxamide synthase, putative; Similar to GB:L42023 SP:P43851 PID:1008795 PID:1205955 PID:1221880; identified by sequence similarity; putative; Belongs to the SAICAR synthetase family.
  
 
 0.989
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.