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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
AMB84753.1succinyl-CoA--3-ketoacid-CoA transferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (219 aa)    
Predicted Functional Partners:
AMB88223.1
succinyl-CoA--3-ketoacid-CoA transferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
AMB85835.1
3-oxoadipate--succinyl-CoA transferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.996
AMB84752.1
acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
  
 
 0.984
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.
  
 0.891
AMB84745.1
acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
  
 
 0.751
AMB85837.1
Catalyzes the thiolytic cleavage of beta-ketoadipyl-CoA to succinate and acetyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
  
 
 0.751
AMB87292.1
acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
  
 
 0.751
fadA
3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
  
 
 0.751
lcdH
3-hydroxybutyryl-CoA dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3- dehydrocarnitine.
  
 
 0.737
AMB83830.1
NADPH:quinone reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.692
Your Current Organism:
Pseudomonas agarici
NCBI taxonomy Id: 46677
Other names: ATCC 25941, CCUG 32769, CFBP 2063, CIP 106703, DSM 11810, ICMP 2656, JCM 12566, LMG 2112, LMG:2112, NCPPB 2289, P. agarici
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