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
frdASimilar to Escherichia coli fumarate reductase flavoprotein subunit FrdA or b4154 SWALL:FRDA_ECOLI (SWALL:P00363) (601 aa) fasta scores: E(): 4.9e-203, 84.52% id in 601 aa. (598 aa)    
Predicted Functional Partners:
frdB
Fumarate reductase iron-sulfur protein; Similar to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri fumarate reductase iron-sulfur protein frdB or b4153 or c5241 or z5760 or ecs5134 or sf4311 SWALL:FRDB_ECOLI (SWALL:P00364) (243 aa) fasta scores: E(): 2.8e-84, 85.24% id in 244 aa; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.999
frdC
Fumarate reductase 15 kDa hydrophobic protein; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.
 
 0.997
sdhB
Similar to Escherichia coli succinate dehydrogenase iron-sulfur protein SdhB or b0724 SWALL:DHSB_ECOLI (SWALL:P07014) (238 aa) fasta scores: E(): 6.3e-88, 87.81% id in 238 aa; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.996
frdD
Fumarate reductase 13 kDa hydrophobic protein; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.
 
 0.996
sdhC
Similar to Escherichia coli, and Escherichia coli O157:H7 succinate dehydrogenase cytochrome b-556 subunit SdhC or CybA or b0721 or z0875 or ecs0746 SWALL:DHSC_ECOLI (SWALL:P10446) (129 aa) fasta scores: E(): 1.1e-38, 79.06% id in 129 aa.
  
 0.989
fumA
Fumarate hydratase class I, aerobic; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.981
sdhD
Succinate dehydrogenase hydrophobic membrane anchor protein; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
  
 0.973
ECA0824
Similar to Rhodospirillum rubrum pyruvate-flavodoxin oxidoreductase NifJ SWALL:NIFJ_RHORU (SWALL:Q53046) (1191 aa) fasta scores: E(): 0, 54.73% id in 1182 aa, and to Escherichia coli probable pyruvate-flavodoxin oxidoreductase ydbk or b1378 SWALL:NIFJ_ECOLI (SWALL:P52647) (1174 aa) fasta scores: E(): 0, 78.79% id in 1174 aa. Also similar to ECA2957 (47.377% id. in 1182 aa overlap).
  
 
 0.961
sucD
succinyl-CoA synthetase alpha 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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
 
 0.958
nuoC
NADH-quinone oxidoreductase chain 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.
  
 
 0.958
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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