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
aceKIsocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. (608 aa)    
Predicted Functional Partners:
AEB85284.1
TIGRFAM: Isocitrate dehydrogenase NADP-dependent, prokaryotic; KEGG: aav:Aave_2572 isocitrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase.
 
 
 
 0.912
AEB85180.1
TIGRFAM: Isocitrate lyase; KEGG: dia:Dtpsy_1447 isocitrate lyase; PFAM: Isocitrate lyase/phosphorylmutase.
 
  
 0.901
AEB86491.1
TIGRFAM: Thiolase; KEGG: ctt:CtCNB1_0487 acetyl-CoA acetyltransferase; PFAM: Thiolase, N-terminal; Thiolase, C-terminal; Belongs to the thiolase-like superfamily. Thiolase family.
       0.837
AEB86493.1
Carbonate dehydratase; Reversible hydration of carbon dioxide. Belongs to the beta-class carbonic anhydrase family.
       0.655
AEB86490.1
PFAM: Short-chain dehydrogenase/reductase SDR; KEGG: dia:Dtpsy_3053 short chain dehydrogenase.
       0.591
AEB86489.1
KEGG: ajs:Ajs_3774 acyl-CoA dehydrogenase domain-containing protein; PFAM: Acyl-CoA oxidase/dehydrogenase, type 1; Acyl-CoA oxidase/dehydrogenase, central domain; Acyl-CoA dehydrogenase, N-terminal.
       0.544
glcB
Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily.
  
  
 0.514
AEB86494.1
KEGG: ajs:Ajs_3779 isovaleryl-CoA dehydrogenase; PFAM: Acyl-CoA oxidase/dehydrogenase, type 1; Acyl-CoA oxidase/dehydrogenase, central domain; Acyl-CoA dehydrogenase, N-terminal.
       0.507
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.