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
sucASWISSPROT P0AFG3: 2-oxoglutarate dehydrogenase E1 component; PIR: PIRSF000157 - 2-oxoglutarate dehydrogenase, E1 component; TIGRFAM: TIGR00239 2-oxoglutarate dehydrogenase, E1 component; COG: COG0567 - 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes; PFAM: PF00676, PF02779. (987 aa)    
Predicted Functional Partners:
lpdA
SWISSPROT P0A9P0: Dihydrolipoyl dehydrogenase; PFAM: PF00364, PF00070, PF02852, PF07992; PROSITE: PS50968, PS00189, PS00076; PRINTS: PR00945, PR00411, PR00368; TIGRFAM: TIGR01350 dihydrolipoamide dehydrogenase; COG: COG1249 - Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase (E3) component, and related enzymes.
  
 0.999
sucB
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; 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).
 0.999
lpd
SWISSPROT P14218: Dihydrolipoyl dehydrogenase; TIGRFAM: TIGR01350 dihydrolipoamide dehydrogenase; COG: COG1249 - Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase (E3) component, and related enzymes; PFAM: PF00070, PF02852, PF07992; PRINTS: PR00945, PR00411, PR00368.
 
 0.990
pdhB2
Pyruvate dehydrogenase E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
  
 0.987
sucC1
succinyl-CoA synthetase beta chain; 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.
 
 0.986
aceF
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.983
lpdV
SWISSPROT Q9I1L9: Dihydrolipoyl dehydrogenase; TIGRFAM: TIGR01350; PFAM: PF00070, PF02852, PF07992.
  
 0.979
pdhC1
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.977
pdhC2
Dihydrolipoamide acetyltransferase; PFAM: alpha/beta hydrolase fold; biotin/lipoyl attachment domain-containing protein; E3 binding domain protein; middle swissprot hit to Acetoin dehydrogenase E2 component from Pseudomonas putida; high Ref YP hit to branched-chain alpha-keto acid dehydrogenase subunit E2 from Sinorhizobium medicae WSM419; unsure GC frame plot; pyruvate dehydrogenase E2 component.
 
 0.962
sdhB
Swiss-Prot: P07014-Succinate dehydrogenase iron-sulfur subunit TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein KEGG: rde:RD1_1630 succinate dehydrogenase, iron-sulfur protein; iron-sulfur subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 
 0.950
Your Current Organism:
Dinoroseobacter shibae
NCBI taxonomy Id: 398580
Other names: D. shibae DFL 12 = DSM 16493, Dinoroseobacter shibae DFL 12, Dinoroseobacter shibae DFL 12 = DSM 16493, Dinoroseobacter shibae DSM 16493, Dinoroseobacter shibae DSM 16493 = DFL 12, Jannaschia sp. DFL-12
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