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
AKX44809.1Dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (546 aa)    
Predicted Functional Partners:
aceE
Pyruvate dehydrogenase; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.998
AKX44479.1
E3 component of 2-oxoglutarate dehydrogenase complex; catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.992
AKX44108.1
Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.984
AKX45496.1
2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.970
AKX44481.1
2-oxoglutarate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.968
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.
  
 0.950
AKX44846.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
  
 
 0.949
AKX45497.1
3-methyl-2-oxobutanoate dehydrogenase; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
 0.925
sucC
succinyl-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.
 
 0.921
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.
 
 0.911
Your Current Organism:
Oblitimonas alkaliphila
NCBI taxonomy Id: 1697053
Other names: CCUG 67636, DSM 100830, O. alkaliphila, Oblitimonas alkaliphila Drobish et al. 2016, Pseudomonadaceae bacterium B4199, Pseudomonadaceae bacterium C6819, Pseudomonadaceae bacterium C6918, Pseudomonadaceae bacterium D2441, Pseudomonadaceae bacterium D3318, Pseudomonadaceae bacterium E1086, Pseudomonadaceae bacterium E1148, Pseudomonadaceae bacterium E5571, bacterium B4199, bacterium C6819, bacterium C6918, bacterium D2441, bacterium D3318, bacterium E1086, bacterium E1148, bacterium E5571, strain B4199
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