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
guaAGMP synthetase; Catalyzes the synthesis of GMP from XMP. (536 aa)    
Predicted Functional Partners:
guaB
Guanosine monophosphate reductase; 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.
 
 0.999
KRU22947.1
Adenine phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.992
gltB
Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.990
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.
  
  
 0.988
argS
arginyl-tRNA synthetase; Catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.988
rplK
50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
    0.981
gatB
glutamyl-tRNA amidotransferase; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
  
 
 0.978
pyrG
CTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
  
 0.978
KRU21490.1
Non-canonical purine NTP pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
 
 
 0.977
gmk
Guanylate kinase; Essential for recycling GMP and indirectly, cGMP.
 
 
 0.976
Your Current Organism:
Psychrobacter piscatorii
NCBI taxonomy Id: 554343
Other names: JCM 15603, NCIMB 14510, P. piscatorii, Psychrobacter piscatorii Yumoto et al. 2010, Psychrobacter sp. JCM 15603, Psychrobacter sp. T-3-2, strain T-3-2
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