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
fadKAMP-dependent synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (518 aa)    
Predicted Functional Partners:
AKL36168.1
Non-ribosomal peptide synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.957
AKL35724.1
Long-chain fatty acid--CoA ligase; Activates fatty acids by binding to coenzyme A; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.926
AKL34556.1
acetyl-CoA acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
  
 
 0.848
AKL34558.1
CoA-transferase; CoA transferase having broad substrate specificity for short- chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Belongs to the 3-oxoacid CoA-transferase family.
  
  
 0.802
AKL34557.1
3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.797
fadB
Multifunctional fatty acid oxidation complex subunit alpha; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
  
 
 0.733
fadJ
Multifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
  
 
 0.733
acs
acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
 
 
0.716
AKL36167.1
Thioester reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.714
entF
Enterobactin synthase subunit F; With EntB, EntD, and EntE forms the multienzyme complex enterobactin synthase; EntF is the serine activating enzyme which catalyzes the formation of the amide and ester bonds of the cyclic enterobactin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.686
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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