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
sucCsuccinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (389 aa)    
Predicted Functional Partners:
sucD
succinyl-CoA synthetase subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
 0.999
odhB
Dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 0.988
AMQ94460.1
Fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 0.987
frdA
Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.985
sucA
2-oxoglutarate dehydrogenase subunit E1; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.964
aceF
Hypothetical protein; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.938
adhE
Acetaldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
  
 0.917
frdD
Fumarate reductase; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.
     
 0.913
frdC
Fumarate reductase; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane; Belongs to the FrdC family.
     
  0.900
AMQ93251.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
  
 
 0.881
Your Current Organism:
Aggregatibacter actinomycetemcomitans
NCBI taxonomy Id: 714
Other names: A. actinomycetemcomitans, ATCC 33384, Actinobacillus (Haemophilus) actinomycetemcomitans, Actinobacillus actinomycetemcomitans, Bacterium acetinomycetum comitans, Bacterium actinomycetem comitans, Bacterium comitans, CCUG 13227, CIP 52.106, DSM 8324, Haemophilus actinomycetemcomitans, Haemophilus actinomyceticomitans, NCTC 9710
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