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
OAZ12992.1acryloyl-CoA reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (332 aa)    
Predicted Functional Partners:
OAZ14909.1
Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aldehyde dehydrogenase family.
   
 0.864
OAZ08515.1
Methylmalonate-semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.864
OAZ15241.1
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; Belongs to the enoyl-CoA hydratase/isomerase family.
   
 0.863
OAZ13223.1
enoyl-CoA hydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.863
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
    
 0.860
OAZ14841.1
AMP-dependent synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.851
acsA
acetyl-CoA 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.
   
 
 0.851
prpE
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.
   
 
 0.851
OAZ08355.1
acetyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.850
OAZ14781.1
acyl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.792
Your Current Organism:
Thalassospira profundimaris
NCBI taxonomy Id: 502049
Other names: CGMCC 1.3997, DSM 17430, T. profundimaris, Thalassospira profundimaris Liu et al. 2007, Thalassospira sp. 35, Thalassospira sp. MCCC 1A00350, Thalassospira sp. MCCC 1A00385, Thalassospira sp. MCCC 1A01166, Thalassospira sp. MCCC 1A01318, Thalassospira sp. MCCC 1A02030, Thalassospira sp. PR54-5, Thalassospira sp. R4-5, Thalassospira sp. R8-17, Thalassospira sp. S25-3-2, strain WP0211
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