STRINGSTRING
STRING protein interaction network
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CG50_14750enoyl-ACP reductase; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. (262 aa)    
Predicted Functional Partners:
CG50_14745
FabB, beta-Ketoacyl-ACP synthase I, KASI; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
 
 0.989
CG50_14155
ACP S-malonyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.963
CG50_14740
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.
  
 
 0.960
CG50_06170
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 0.945
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
  
 0.938
CG50_14340
beta-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
 
 0.894
CG50_14180
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 
 
 0.892
fabZ
3-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.
 
 
 0.854
accA
acetyl-CoA carboxylase subunit alpha; 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.
  
  
 0.767
fabH
3-oxoacyl-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 superfamily. FabH family.
 
 
 0.708
Your Current Organism:
Paenirhodobacter enshiensis
NCBI taxonomy Id: 1105367
Other names: CCTCC AB 2011145, KCTC 15169, P. enshiensis, Paenirhodobacter enshiensis Wang et al. 2014, Rhodobacter sp. DW2-9, strain DW2-9
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