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tesA tesA ybbO ybbO tesB tesB fadD fadD ybbP ybbP fadE fadE fadM fadM ybbN ybbN fabB fabB fabZ fabZ fabF fabF
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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tesAacyl-CoA thioesterase 1 and protease I and lysophospholipase L1; TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease. TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA. TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate. Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin [...] (208 aa)    
Predicted Functional Partners:
ybbO
Putative oxidoreductase; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
 
  
 0.977
tesB
acyl-CoA thioesterase 2; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known; Belongs to the C/M/P thioester hydrolase family.
   
  
 0.921
fadD
acyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source.
 
   
 0.921
ybbP
Putative ABC transporter permease; Putative oxidoreductase.
 
     0.911
fadE
Acyl coenzyme A dehydrogenase; Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth.
      
 0.879
fadM
Long-chain acyl-CoA thioesterase III; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids; Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
   
  
 0.879
ybbN
DnaK co-chaperone, thioredoxin-like protein; Chaperedoxin that combines a chaperone activity with a redox- protective function. Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation. Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes. After bleach stress, it transfers its substr [...]
 
    0.871
fabB
3-oxoacyl-[acyl-carrier-protein] synthase I; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
   
  
 0.831
fabZ
(3R)-hydroxymyristol acyl carrier protein dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
     
 0.830
fabF
3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
      
 0.828
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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