close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
aroEShikimate dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). (274 aa)    
Predicted Functional Partners:
aroK
Shikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family.
 
 0.999
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
  
 0.998
aroD
3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. Belongs to the type-I 3-dehydroquinase family.
  
 0.998
aroB
3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
  
 0.983
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
  
 0.954
AEH23583.1
Phosphoribosylaminoimidazolecarboxamide formyltransferase; KEGG: dte:Dester_0983 bifunctional purine biosynthesis protein PurH; PFAM: MGS-like; AICARFT/IMPCHase bienzyme, formylation region.
       0.811
AEH23586.1
KEGG: dal:Dalk_3859 ATPase AAA-2 domain protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpX chaperone family.
  
  
 0.802
AEH23584.1
KEGG: sfu:Sfum_3056 radical SAM domain-containing protein; PFAM: Radical SAM; SMART: Elongator protein 3/MiaB/NifB.
  
    0.795
AEH23578.1
KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein.
       0.778
AEH23585.1
PFAM: Signal transduction response regulator, receiver region; KEGG: dth:DICTH_1976 response regulator receiver sensor signal transduction histidine kinase.
       0.773
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
Server load: medium (54%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.