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fabV protein (Idiomarina loihiensis) - STRING interaction network
"fabV" - trans-2-enoyl-CoA reductase in Idiomarina loihiensis
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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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fabVtrans-2-enoyl-CoA reductase; Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP) (392 aa)    
Predicted Functional Partners:
fabZ
(3R)-hydroxymyristoyl-ACP 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 (151 aa)
   
 
  0.963
fabB
3-oxoacyl-ACP synthase (404 aa)
   
 
  0.960
fabA
3-hydroxydecanoyl-ACP dehydratase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl- ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)- decenoyl-ACP. Can catalyze the dehydratase reaction for beta- hydroxyacyl-ACPs with saturated chain lengths up to 16-0, being most active on intermediate chain length (170 aa)
   
 
  0.959
IL0143
3-oxoacyl-ACP synthase (412 aa)
   
 
  0.939
IL0140
3-oxoacyl-ACP synthase (397 aa)
   
 
  0.936
fadJ
Multifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities (708 aa)
         
    0.900
fadB
Fatty acid oxidation complex alpha subunit; 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 (718 aa)
         
    0.900
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (310 aa)
         
    0.800
lipB
Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (221 aa)
         
    0.800
IL0180
Ferredoxin (65 aa)
       
      0.642
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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