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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
bfmBABDihydrolipoyllysine-residue (2-methylpropanoyl) transferase, E2 component; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). This protein is the E2 component and catalyzes the reaction: 2-methylpropanoyl-CoA + enzyme 6-N-(dihydrolipoyl)lysine = CoA + enzyme 6-N-(S-(2-methylpr [...] (450 aa)    
Predicted Functional Partners:
sucA
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3); High confidence in function and specificity.
 0.999
bkdA1
2-Oxoisovalerate dehydrogenase, E1 component; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. This complex contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 component displays a modular architecture. The N-terminal domain is a dehydrogenase and the C-terminal domain belongs to the transketolase family. Both activities [...]
 0.999
bkdA2
2-Oxoisovalerate dehydrogenase, E1 component; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. This complex contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 component displays a modular architecture. The N-terminal domain is a dehydrogenase and the C-terminal domain belongs to the transketolase family. Both activities [...]
 0.999
bfmBC
The Dihydrolipoyl dehydrogenase is the E3 component of the branched-chain alpha-keto dehydrogenase complex. This complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched- chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E3 component converts the Protein 6-N-(dihydrolipoyl)lysine to protein 6-N-(lipoyl)lysine. Dihydrolipoyl dehydrogenase is a homodimer, which binds 1 NAD [...]
 0.996
pdhD
Dihydrolipoyl dehydrogenase, E3 component; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, linking glycolysis to the tricarboxylic acid cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). PdhD is the E3 component. It catalyzes the oxidation of dihydrolipoamide to lipoamide. PdhD is a homodimer which binds 1 NADP and 1 FAD per subunit; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family; Localiz [...]
 0.995
sucC
Succinyl-CoA ligase [ADP-forming] 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.
 
 0.977
pdhB
Pyruvate dehydrogenase, E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
 0.977
sucD
Succinyl-CoA ligase [ADP-forming] 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.
 
 0.972
pdhA
Pyruvate dehydrogenase, E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.949
sucB
Dihydrolipoamide succinyltransferase E2 component; 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).
  
  
 
0.919
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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