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
KRU22519.1Quinone oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)    
Predicted Functional Partners:
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.
  
 0.939
KRU22796.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
     
 0.935
KRU22020.1
Catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.934
KRU21689.1
enoyl-CoA hydratase; Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.934
acsA
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA 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; Belongs to the ATP-dependent AMP-binding enzyme family.
   
 
  0.929
prpE
propionate--CoA ligase; Catalyzes the formation of propionyl-CoA using propionate as a substrate; PrpE from Ralstonia solanacearum can produce acetyl-, propionyl-, butyryl- and acrylyl-coenzyme A, and Salmonella enterica produces propionyl- and butyryl-coenzyme A; not expressed in Escherichia coli when grown on propionate/minimal media; ATP-dependent; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.929
KRU22040.1
AMP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.929
KRU21464.1
3-hydroxyacyl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the enoyl-CoA hydratase/isomerase family.
  
 0.868
KRU22688.1
Methylmalonate-semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.858
KRU22677.1
Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aldehyde dehydrogenase family.
   
  0.742
Your Current Organism:
Psychrobacter piscatorii
NCBI taxonomy Id: 554343
Other names: JCM 15603, NCIMB 14510, P. piscatorii, Psychrobacter piscatorii Yumoto et al. 2010, Psychrobacter sp. JCM 15603, Psychrobacter sp. T-3-2, strain T-3-2
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