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
fadH2,4-dienoyl-CoA reductase; Catalyzes the formation of trans-2- enoyl-CoA from 2,4-dienoyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. (675 aa)    
Predicted Functional Partners:
gltB
Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.999
AMQ42866.1
Electron transporter RnfB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.967
AMQ42865.1
Electron transfer flavoprotein subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.929
AMQ41773.1
(Fe-S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.826
AMQ45098.1
Flavodoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.805
fre
NAD(P)H-flavin reductase; catalyzes the reversible oxidation/reduction of NAD(P) and flavine mononucleotide; in Salmonella and E. coli this protein also reduces aquacob(III)alamin to cob(II)alamin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.758
AMQ42947.1
Sulfite reductase; With AsrAC catalyzes the reduction of sulfite to hydrogen sulfide; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.758
fadB
Multifunctional fatty acid oxidation complex subunit alpha; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
 
  
 0.728
AMQ42550.1
Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.722
fdx
2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.722
Your Current Organism:
Aeromonas veronii
NCBI taxonomy Id: 654
Other names: A. veronii, ATCC 35624, ATCC 49904 [[Aeromonas ichthiosmia]], Aeromonas culicicola, Aeromonas culicicola Pidiyar et al. 2002, Aeromonas hybridization group 10 (HG10), Aeromonas ichthiosmia, Aeromonas sp. G18, Aeromonas sp. R1, Aeromonas sp. R9, Aeromonas sp. TH074, Aeromonas sp. TH076, CCUG 27821, CECT 4257, CECT 4486 [[Aeromonas ichthiosmia]], CIP 103438, CIP 104613 [[Aeromonas ichthiosmia]], CIP 107763 [[Aeromonas culicicola]], DSM 6393 [[Aeromonas ichthiosmia]], DSM 7386, Enteric Group 77, JCM 7375, JCM 8354 [[Aeromonas ichthiosmia]], LMG 12645 [[Aeromonas ichthiosmia]], LMG:12645 [[Aeromonas ichthiosmia]], MTCC 3249 [[Aeromonas culicicola]], NCIMB 13205 [[Aeromonas ichthiosmia]], NICM 5147 [[Aeromonas culicicola]], strain 115/II [[Aeromonas ichthiosmia]]
Server load: medium (50%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.