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sucB protein (Acinetobacter baumannii) - STRING interaction network
"sucB" - Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex in Acinetobacter baumannii
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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Score
sucBDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (398 aa)    
Predicted Functional Partners:
sucA
Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component; Derived by automated computational analysis using gene prediction method- Protein Homology (946 aa)
  0.999
sucC
Succinate--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 (388 aa)
  0.999
sucD
Succinate--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 (296 aa)
  0.998
AIL78966.1
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 (477 aa)
  0.997
lpdA
E3 component of alpha keto acid dehydrogenase complexes LpdC; forms a homodimer; binds one molecule of FAD monomer; catalyzes NAD+-dependent oxidation of dihydrolipoyl cofactors that are covalently linked to the E2 component; Derived by automated computational analysis using gene prediction method- Protein Homology (467 aa)
  0.993
AIL79243.1
Derived by automated computational analysis using gene prediction method- Protein Homology (457 aa)
  0.964
AIL80403.1
Acyl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (406 aa)
   
  0.913
cat1
Propionyl-CoA--succinate CoA transferase; Derived by automated computational analysis using gene prediction method- Protein Homology (504 aa)
     
    0.912
AIL80693.1
Alpha-ketoacid dehydrogenase subunit beta; Derived by automated computational analysis using gene prediction method- Protein Homology (339 aa)
 
  0.906
AIL80692.1
ABC transporter substrate-binding protein; Derived by automated computational analysis using gene prediction method- Protein Homology (320 aa)
 
 
  0.868
Your Current Organism:
Acinetobacter baumannii
NCBI taxonomy Id: 470
Other names: A. baumannii, ATCC 19606, Acinetobacter baumannii, Acinetobacter genomosp. 2, Acinetobacter genomospecies 2, Bacterium anitratum, CCUG 19096, CIP 70.34, DSM 30007, JCM 6841, NCCB 85021, NCTC 12156
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