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
fccAFlavocytochrome c; Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional (By similarity); In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (583 aa)    
Predicted Functional Partners:
Sfri_2156
Fumarase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.982
Sfri_0458
Succinate dehydrogenase subunit B; KEGG: son:SO0399 fumarate reductase iron-sulfur protein; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.980
Sfri_0678
Succinate dehydrogenase subunit B; KEGG: son:SO0399 fumarate reductase iron-sulfur protein; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.980
Sfri_0456
KEGG: son:SO0396 fumarate reductase cytochrome B subunit.
  
 0.974
Sfri_0680
KEGG: son:SO0396 fumarate reductase cytochrome B subunit.
  
 0.974
Sfri_0229
PFAM: fumarate lyase; KEGG: vch:VC1573 fumarate hydratase, class II.
 
 0.954
sucD
succinyl-CoA synthetase (ADP-forming) 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.
 
 0.922
Sfri_0679
KEGG: son:SO0398 fumarate reductase flavoprotein subunit; TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein.
  
  
0.918
Sfri_0457
KEGG: son:SO0398 fumarate reductase flavoprotein subunit; TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein.
  
  
0.917
sucC
succinyl-CoA synthetase (ADP-forming) 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.
  
 0.910
Your Current Organism:
Shewanella frigidimarina
NCBI taxonomy Id: 318167
Other names: S. frigidimarina NCIMB 400, Shewanella frigidimarina NCIMB 400, Shewanella frigidimarina str. NCIMB 400, Shewanella frigidimarina strain NCIMB 400
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