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
sucA2-oxoglutarate decarboxylase, thiamine-requiring E1 subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : TCA cycle. (943 aa)    
Predicted Functional Partners:
sucB
2-oxoglutarate dehydrogenase dihydrolipoyltranssuccinylase subunit; 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
sucC
succinyl-CoA synthetase, beta subunit glutaryl-CoA synthetase, beta subunit; 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.
 0.995
lpdG
Dihydrolipoyl dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid.
 
 0.995
sucD
succinyl-CoA synthetase alpha subunit; 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.
 0.990
aceF
AceF-S-acetyldihydrolipoate; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.988
lpd
Dihydrolipoyl dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid.
 
 0.987
lpdV
Dihydrolipoyl dehydrogenase component of branched-chain alpha-keto acid dehydrogenase complex; Function experimentally demonstrated in the studied species; enzyme; Fattyacidandphospholipidmetabolism : Degradation.
 
 0.983
icd
Isocitrate dehydrogenase, NADP(+)-specific; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Anaerobic.
   
 
 0.981
nuoC
NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
   
 
 0.964
sdhB
Succinate dehydrogenase iron-sulfur subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Aerobic.
 
 0.964
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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