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
AEB86841.1PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase; KEGG: ajs:Ajs_3978 glyoxalase/bleomycin resistance protein/dioxygenase. (133 aa)    
Predicted Functional Partners:
AEB86840.1
KEGG: ajs:Ajs_3977 3-ketoacyl-(acyl-carrier-protein) reductase; PFAM: Short-chain dehydrogenase/reductase SDR.
  
 
 0.765
AEB86839.1
PFAM: Glutathione S-transferase, N-terminal; Glutathione S-transferase, C-terminal; KEGG: ajs:Ajs_3976 glutathione S-transferase domain-containing protein; Belongs to the GST superfamily.
  
  
 0.721
AEB86842.1
SMART: DNA topoisomerase, type IA, DNA-binding; SWIB domain; DNA topoisomerase, type IA, domain 2; Toprim domain; TIGRFAM: DNA topoisomerase III, bacterial-type; KEGG: ajs:Ajs_3990 DNA topoisomerase III; PFAM: DNA topoisomerase, type IA, central; SWIB/MDM2 domain; Toprim domain.
     
 0.642
AEB86844.1
KEGG: dia:Dtpsy_3341 biotin/acetyl-CoA-carboxylase ligase; TIGRFAM: Biotin--acetyl-CoA-carboxylase ligase; PFAM: Biotin/lipoate A/B protein ligase; Biotin protein ligase, C-terminal.
  
    0.585
AEB84583.1
KEGG: dia:Dtpsy_2283 succinate dehydrogenase, cytochrome b556 subunit; TIGRFAM: Succinate dehydrogenase, cytochrome b556 subunit; PFAM: Succinate dehydrogenase/Fumarate reductase, transmembrane subunit.
  
  
 0.496
nuoD
NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
  
  
 0.484
AEB86088.1
PFAM: Nitroreductase-like; KEGG: dia:Dtpsy_0966 nitroreductase.
 
  
 0.472
AEB83456.1
PFAM: 4Fe-4S binding domain; KEGG: ajs:Ajs_3467 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein.
  
  
 0.471
AEB84629.1
KEGG: ajs:Ajs_2522 short-chain dehydrogenase/reductase SDR; PFAM: Short-chain dehydrogenase/reductase SDR; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
 
 
 0.461
AEB86843.1
KEGG: dia:Dtpsy_3340 nuclear protein SET; PFAM: SET domain; SMART: SET domain; Post-SET domain.
       0.455
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 (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.