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
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[Homology]
Score
sucDSuccinyl-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. (290 aa)    
Predicted Functional Partners:
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.
 0.999
sdhB
Succinate dehydrogenase is a complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558. It is involved in the citrate cycle and catalyzes the reaction: succinate + acceptor = fumarate + reduced acceptor. It uses a FAD as a cofactor. SdhB is the iron-sulfur subunit. Localized in the cytoplasm; High confidence in function and specificity.
  
 0.984
sdhA
Succinate dehydrogenase is a complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558. It is involved in the citrate cycle and catalyzes the reaction: succinate + acceptor = fumarate + reduced acceptor. It uses a FAD as a cofactor. SdhA is the flavoprotein subunit. Localized in the cytoplasm; High confidence in function and specificity.
 
 0.980
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).
 0.978
bfmBAB
Dihydrolipoyllysine-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 [...]
 
 0.972
pdhC
Dihydrolipoyllysine-residue acetyltransferase, PDH complex E2 component; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.945
mutB
Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.942
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.
 
 0.920
sdhC
Succinate dehydrogenase is a complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558. It is involved in the citrate cycle and catalyzes the reaction: succinate + acceptor = fumarate + reduced acceptor. It uses a FAD as a cofactor. SdhC is the cytochrome b558 subunit. It binds two hemes. Features five transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity.
    
 0.918
mutA
Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.916
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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