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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
AJE18002.13-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (408 aa)    
Predicted Functional Partners:
fabG
3-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.989
fabD
Malonyl CoA-ACP transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.985
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.
 
 
 0.977
fabG-2
3-ketoacyl-ACP 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.
 
 0.969
AJE19286.1
enoyl-ACP reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.964
AJE17998.1
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.
 
  
 
0.954
AJE18008.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.936
AJE18001.1
Thioester dehydrase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.935
AJE18093.1
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.
  
  
 
0.927
fabF
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.
  
  
 
0.925
Your Current Organism:
Neisseria elongata
NCBI taxonomy Id: 546263
Other names: N. elongata subsp. glycolytica ATCC 29315, Neisseria elongata subsp. glycolytica ATCC 29315, Neisseria elongata subsp. glycolytica str. ATCC 29315, Neisseria elongata subsp. glycolytica strain ATCC 29315
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