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
Rta_04120Candidate 3-oxoacyl-[acyl-carrier-protein] synthase (Beta-ketoacyl-ACP synthase). (648 aa)    
Predicted Functional Partners:
fabD
Candidate [Acyl-carrier-protein] S-malonyltransferase.
  
 
 0.975
fabF
Candidate 3-oxoacyl-[acyl-carrier-protein] synthase (Beta-ketoacyl-ACP synthase); Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 
 
 0.971
fabB
Candidate 3-oxoacyl-[acyl-carrier-protein] synthase I (Beta-ketoacyl-ACP synthase); Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
 
 0.970
Rta_04110
Conserved hypothetical protein.
 
     0.947
accD
Candidate Acetyl-CoA carboxylase carboxyl transferase, beta subunit; 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.
 
 
 0.947
accA
Candidate Acetyl-CoA carboxylase, alpha subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
 
 
 0.946
accB
Candidate Biotin carboxyl carrier protein of acetyl-CoA carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
 
 0.945
fabH
Candidate 3-oxoacyl-[acyl-carrier-protein] synthase (Beta-ketoacyl-ACP synthase); 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 sup [...]
  
  
0.929
accC
Candidate Biotin carboxylase (subunit of acetyl-CoA carboxylase); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 
 0.926
Rta_02640
3-oxoacyl-[acyl-carrier-protein] reductase-like protein; Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases).
  
 
 0.909
Your Current Organism:
Ramlibacter tataouinensis
NCBI taxonomy Id: 365046
Other names: Acidivorax sp. TTB310, Acidovorax sp. TTB310, R. tataouinensis TTB310, Ramlibacter tataouinensis TTB310, Ramlibacter tataouinensis str. TTB310, Ramlibacter tataouinensis strain TTB310
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.