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
caiAcrotonobetainyl-CoA:carnitine CoA-transferase; Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA; Belongs to the acyl-CoA dehydrogenase family. (380 aa)    
Predicted Functional Partners:
nuoC
NADH:ubiquinone oxidoreductase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
 0.999
fixB
Hypothetical protein; Required for anaerobic carnitine reduction. May bring reductant to CaiA.
 
 0.998
fixA
Electron transfer flavoprotein; Required for anaerobic carnitine reduction. May bring reductant to CaiA.
 
 
 0.985
AKH88340.1
Catalyzes the dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the enoyl-CoA hydratase/isomerase family.
 
 0.985
CaiB
crotonobetainyl-CoA:carnitine CoA-transferase; Catalyzes formation of L-carnitinyl-CoA by transfering the CoA moiety from gamma-butyrobetainyl-CoA, also catalyzes the formation of crotonobetainyl-CoA by transfer of CoA from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CoA-transferase III family.
 
 
 0.981
AKH88862.1
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.
 
 0.899
nifJ-2
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.891
caiC
crotonobetainyl-CoA:carnitine CoA-transferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.874
AKH88332.1
Ferredoxin; Could be a 3Fe-4S cluster-containing protein.
 
 
 0.849
nuoA
NADH:ubiquinone oxidoreductase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family.
    
 0.822
Your Current Organism:
Edwardsiella tarda
NCBI taxonomy Id: 636
Other names: ATCC 15947, ATCC 23656, CIP 78.61, DSM 30052, E. tarda, Edwardsiella anguillimortifera, Edwardsiella sp. HMK1, Edwardsiella sp. PB46, LMG 2793, LMG:2793, NBRC 105688, NCCB 73021, NCTC 10396, Paracolobactrum anguillimortiferum
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