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
KOH22237.1Dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. (226 aa)    
Predicted Functional Partners:
KOH21415.1
Epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.742
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.
  
 0.734
fadJ
Multifunctional fatty acid oxidation complex subunit alpha; Multifunctional enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase; catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA; exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities: forms a heterotetramer with FadI; similar to FadA2B2 complex; involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.734
KOH24990.1
Catalase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the catalase family.
   
 0.721
KOH22820.1
Catalase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.721
KOH23956.1
biotin--[acetyl-CoA-carboxylase] synthetase; Catalyzes the formation of biotinyl-5'-AMP, also acts as a transcriptional repressor of the biotin operon; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.670
KOH22738.1
Flavodoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.626
KOH18203.1
Acetaldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.623
fadA
3-ketoacyl-CoA thiolase; FadA; fatty acid oxidation complex component beta; functions in a heterotetramer with FadB; similar to FadI2J2 complex; functions in beta-oxidation of fatty acids; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
  
 
 0.591
KOH22252.1
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.
  
 
 0.591
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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