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
AFY72780.1PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); e3 binding domain; Biotin-requiring enzyme; TIGRFAM: pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form. (430 aa)    
Predicted Functional Partners:
AFY72438.1
Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
 
 0.999
AFY73175.1
Dihydrolipoamide dehydrogenase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: dihydrolipoamide dehydrogenase.
 0.999
pdhA
Pyruvate dehydrogenase E1 component, alpha subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.999
AFY74942.1
PFAM: Citrate synthase; TIGRFAM: 2-methylcitrate synthase/citrate synthase II; Belongs to the citrate synthase family.
 
 0.983
AFY73014.1
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain.
 0.980
AFY74433.1
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain.
 
 0.977
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
   
 0.934
acsA
acetate--CoA ligase; 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.
  
 
 0.932
AFY73144.1
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 
 0.923
AFY73362.1
acetyl-CoA carboxylase, biotin carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 0.922
Your Current Organism:
Synechococcus sp. PCC7502
NCBI taxonomy Id: 1173263
Other names: S. sp. PCC 7502, Synechococcus sp. PCC 7502, Synechococcus sp. Rippka_B2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.