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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
fabF3-oxoacyl synthase 2; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. (413 aa)    
Predicted Functional Partners:
fabD
Malonyl CoA-acyl carrier protein transacylase.
 0.999
fabH1
3-oxoacyl synthase 3; 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; Belongs to the thiolase-like superfamily. FabH family.
 
 
 0.997
fabG
3-oxoacyl reductase; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
 
 0.995
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
  
 0.990
fabV
Putative 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); Belongs to the TER reductase family.
  
 
 0.979
lipB
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.
     
  0.938
fabZ
(3R)-hydroxymyristoyl-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.
 
 
 0.913
fabA
3-hydroxydecanoyl 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.
  
 
 0.904
accD1
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta 1; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family.
  
 
 0.855
holB
DNA polymerase III subunit delta'.
     
 0.831
Your Current Organism:
Photodesmus katoptron
NCBI taxonomy Id: 28176
Other names: Anomalops katoptron symbiont, C. Photodesmus katoptron, Candidatus Photodesmus katoptron
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.