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
AEB86490.1PFAM: Short-chain dehydrogenase/reductase SDR; KEGG: dia:Dtpsy_3053 short chain dehydrogenase. (222 aa)    
Predicted Functional Partners:
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.
  
  0.777
AEB86223.1
KEGG: app:CAP2UW1_1324 oxidoreductase FAD-binding domain protein; PFAM: Oxidoreductase, FAD-binding domain; Ferredoxin; Cytochrome b/b6, N-terminal; Oxidoreductase FAD/NAD(P)-binding.
  
 0.768
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.
  
 
 0.654
aceK
Isocitrate 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.
       0.591
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.
  
  0.532
AEB86493.1
Carbonate dehydratase; Reversible hydration of carbon dioxide. Belongs to the beta-class carbonic anhydrase family.
     
 0.493
AEB83666.1
TIGRFAM: Malonyl CoA-acyl carrier protein transacylase; KEGG: ajs:Ajs_3279 [acyl-carrier-protein] S-malonyltransferase; PFAM: Acyl transferase.
  
 
 0.490
AEB85897.1
KEGG: dia:Dtpsy_2451 transcriptional regulator, Crp/Fnr family; PFAM: Cyclic nucleotide-binding domain; HTH transcriptional regulator, Crp; SMART: HTH transcriptional regulator, Crp.
  
 
 0.478
AEB86588.1
PFAM: Sulfatase; KEGG: axy:AXYL_03117 arylsulfatase.
   
 
 0.478
AEB83133.1
KEGG: rfr:Rfer_0698 hypothetical protein.
 
 
 0.465
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
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