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
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Score
AARI_05890Putative acyl-CoA dehydrogenase; Possibly involved in the metabolism of lipids. Match to protein domains PF08028, PF02771 and PF02770. Acyl-CoA dehydrogenases catalyze the alpha,beta- dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. (392 aa)    
Predicted Functional Partners:
AARI_01880
enoyl-CoA hydratase catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA.
  
 0.948
AARI_26770
enoyl-CoA hydratase catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA.
  
 0.948
fadA
Fatty acid oxidation complex subunit beta; Also named acetyl-CoA C-acyltransferase. Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. Part of the FadAB fatty acid oxidation complex; Belongs to the thiolase-like superfamily. Thiolase family.
  
 0.935
AARI_15780
Putative acyl-CoA dehydrogenase; Possibly involved in the metabolism of lipids. Match to protein domains PF08028, PF02771 and PF02770. Acyl-CoA dehydrogenases catalyze the alpha,beta- dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD.
  
  
 
0.926
AARI_22150
Putative acyl-CoA dehydrogenase; Possibly involved in the metabolism of lipids. Match to protein domains PF08028, PF02771 and PF02770. Acyl-CoA dehydrogenases catalyze the alpha,beta- dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD.
  
  
 
0.914
AARI_26490
Putative acyl-CoA dehydrogenase; Possibly involved in the metabolism of lipids. Match to protein domains PF08028, PF02771 and PF02770. Acyl-CoA dehydrogenases catalyze the alpha,beta- dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD.
  
  
 
0.914
sucB
Dihydrolipoyllysine-residue succinyltransferase; It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex, which is involved in the TCA cycle.
   
 0.912
lpdA-3
E3 component of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes.
  
 0.910
fadB
Fatty acid oxidation complex subunit alpha; Identified by similarity to protein SP: P21177 (Escherichia coli). Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. Part of the FadAB fatty acid oxidation complex.
 
 0.909
aco
acyl-CoA oxidase; Identified by similarity to potein SP:Q33DR0 (Arthrobacter ureafaciens). Catalyzes the oxidation of acyl-coenzyme A (acyl-CoA) thioester to the corresponding trans-2-enoyl-CoA thioester: acyl-CoA + O2 --> trans-2-enoyl-CoA + H2O2. Probably involved in beta-oxidation of fatty acids.
  
  
 
0.905
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
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