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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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sucDsuccinyl-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. (298 aa)    
Predicted Functional Partners:
AGA69599.1
PFAM: ATP-grasp domain; TIGRFAM: succinyl-CoA synthetase, beta subunit.
 0.999
AGA67597.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: Domain of unknown function; domain; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain.
  
 0.949
AGA70809.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain.
  
 
 0.936
AGA68195.1
PFAM: Citrate synthase; Belongs to the citrate synthase family.
 
 
 0.873
acsA
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
 
 
 0.869
AGA68696.1
NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit; PFAM: NADH-ubiquinone oxidoreductase-F iron-sulfur binding region; Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit; SLBB domain.
  
 
 0.849
nuoC
NADH/F420H2 dehydrogenase, subunit C; 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 a menaquinone. 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; Belongs to the complex I 30 kDa subunit family.
   
 
 0.838
AGA68257.1
acetyl-CoA acetyltransferase; PFAM: Thiolase, C-terminal domain; Thiolase, N-terminal domain; Belongs to the thiolase-like superfamily. Thiolase family.
  
 0.833
AGA69423.1
acetyl-CoA acetyltransferase; PFAM: Thiolase, C-terminal domain; Thiolase, N-terminal domain; TIGRFAM: acetyl-CoA acetyltransferases; Belongs to the thiolase-like superfamily. Thiolase family.
  
 0.833
AGA70121.1
acetyl-CoA acetyltransferase; PFAM: Thiolase, C-terminal domain; Thiolase, N-terminal domain; Belongs to the thiolase-like superfamily. Thiolase family.
  
 0.833
Your Current Organism:
Desulfitobacterium dichloroeliminans
NCBI taxonomy Id: 871963
Other names: D. dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans DCA1, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans LMG P21439, Desulfitobacterium dichloroeliminans str. LMG P-21439, Desulfitobacterium dichloroeliminans strain LMG P-21439
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