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Mettu_3870 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3870" - Enoyl-[acyl-carrier-protein] reductase [NADH] in Methylobacter tundripaludum
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Mettu_3870Enoyl-[acyl-carrier-protein] reductase [NADH] (260 aa)    
Predicted Functional Partners:
Mettu_0825
3-oxoacyl-[acyl-carrier-protein] synthase 2 ; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (414 aa)
   
 
  0.989
Mettu_0698
Beta-ketoacyl-acyl-carrier-protein synthase I (407 aa)
   
 
  0.989
fabZ
Beta-hydroxyacyl-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 (147 aa)
 
 
  0.986
Mettu_3287
Beta-ketoacyl-acyl-carrier-protein synthase I (409 aa)
 
 
  0.985
fabA
Trans-2-decenoyl-[acyl-carrier-protein] isomerase ; 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 (171 aa)
   
 
  0.981
Mettu_3290
Beta-ketoacyl-acyl-carrier-protein synthase I (423 aa)
   
 
  0.973
lipA
Sulfur insertion protein LipA ; 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 (320 aa)
   
 
  0.898
Mettu_0822
Malonyl CoA-acyl carrier protein transacylase (318 aa)
   
   
  0.897
lipB
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase ; 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 (202 aa)
   
 
  0.894
fabH
Beta-ketoacyl-ACP synthase III ; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched- chain and/or straight-chain of fatty acids (322 aa)
 
   
  0.892
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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