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
sucDsuccinyl-CoA synthetase, alpha subunit (sucD); 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. (293 aa)    
Predicted Functional Partners:
sucC
succinyl-CoA synthetase, beta subunit (sucC); 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.
 0.999
frdB
Fumarate reductase, iron-sulfur protein (frdB); Similar to GB:U14003 SP:P00364 GB:J01611 PID:145264 PID:536997 percent identity: 75.51; identified by sequence similarity; putative.
 
 0.963
frdA
Fumarate reductase, flavoprotein subunit (frdA); Similar to GB:U14003 SP:P00363 GB:J01611 PID:145263 PID:536998 percent identity: 75.54; identified by sequence similarity; putative.
 
 0.946
sucA
2-oxoglutarate dehydrogenase E1 component (sucA); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
  
 0.927
fumC
Fumarate hydratase, class II (fumC); Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
  
 0.901
sucB
2-oxoglutarate dehydrogenase E2 component, dihydrolipoamide succinyltransferase(sucB); 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).
  
 0.893
mdh
Malate dehydrogenase (mdh); Catalyzes the reversible oxidation of malate to oxaloacetate.
  
 0.877
maeB
Malate oxidoreductase, putative; Similar to GB:U00096 PID:1788806 PID:1799885 PID:1799887 percent identity: 68.69; identified by sequence similarity; putative; In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.
  
 
 0.842
aceF
Dihydrolipoamide acetyltransferase (aceF); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
  
 0.840
pta
Phosphate acetyltransferase (pta); Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family.
  
 
 0.816
Your Current Organism:
Haemophilus influenzae
NCBI taxonomy Id: 71421
Other names: H. influenzae Rd KW20, Haemophilus influenzae KW20, Haemophilus influenzae Rd, Haemophilus influenzae Rd KW20
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