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
acsAAMP-dependent 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. (653 aa)    
Predicted Functional Partners:
KMJ54249.1
3-hydroxyacyl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.924
KMJ53922.1
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.
  
 0.907
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.
  
 0.899
KMJ54296.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
  
 
 0.864
KMJ52965.1
Malate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the malate synthase family.
   
 0.848
ackA
Acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family.
   
 
 0.844
ackA-2
Acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family.
   
 
 0.844
KMJ52715.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.831
glcB
Malate synthase; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily.
   
 0.813
prpB
2-methylisocitrate lyase; Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate. Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.
  
 
 0.812
Your Current Organism:
Vogesella sp. EB
NCBI taxonomy Id: 1526735
Other names: V. sp. EB
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.