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
gphPhosphoglycolate phosphatase; Specifically catalyzes the dephosphorylation of 2- phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress. Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. (226 aa)    
Predicted Functional Partners:
VC_2625
Ribulose-phosphate 3-epimerase; Similar to SP:P32661 GB:Z19601 PID:41222 GB:U00096 PID:1789788; identified by sequence similarity; putative; Belongs to the ribulose-phosphate 3-epimerase family.
  
  
 0.901
VC_1198
Conserved hypothetical protein; Identified by Glimmer2; putative.
    
 0.864
VC_A0985
Oxidoreductase/iron-sulfur cluster-binding protein; Similar to GB:AE000511 PID:2314381; identified by sequence similarity; putative.
    
 0.864
hisB
Imidazoleglycerol-phosphate dehydratase/histidinol-phosphatase; Similar to SP:P06987 GB:X03416 PID:41696 PID:41711 GB:U00096; identified by sequence similarity; putative; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
    
 0.863
VC_0705
Chorismate mutase/prephenate dehydratase; Similar to GB:L42023 SP:P43900 PID:1006481 PID:1221267 PID:1205390; identified by sequence similarity; putative.
  
 
 0.806
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.
  
 
  0.798
VC_2198
Basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein.
    
   0.793
trpS
tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.788
pta
Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family.
  
 0.777
murP
PTS system, sucrose-specific IIBC component, putative; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring.
    
  0.761
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
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.