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
APW34294.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (77 aa)    
Predicted Functional Partners:
APW35317.1
NADH-quinone oxidoreductase subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
APW34293.1
3-methyl-2-oxobutanoate dehydrogenase subunit VorB; Catalyzes the coenzyme A-dependent oxidation of 3-methyl-2-oxobutanoate coupled to the reduction of ferredoxin producing S-(2-methylpropanoyl)-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.971
APW34292.1
2-oxoglutarate oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.963
APW34291.1
2-oxoglutarate ferredoxin oxidoreductase subunit gamma; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.957
NifJ
Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.920
nuoB
NADH dehydrogenase; 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.
  
 0.881
nuoH
NADH-quinone oxidoreductase subunit H; 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. This subunit may bind ubiquinone.
  
 0.866
APW35311.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.865
nuoA
NADH-quinone oxidoreductase subunit A; 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 subunit 3 family.
  
 0.861
nuoN
Transposase; 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 subunit 2 family.
  
 0.856
Your Current Organism:
Prevotella intermedia
NCBI taxonomy Id: 28131
Other names: ATCC 25611, Bacteroides intermedius, Bacteroides melaninogenicus subsp. intermedius, CCUG 24041, CIP 101222, CIP 103682, DSM 20706, JCM 11150, JCM 12248, NCTC 13070, P. intermedia, VPI 4197, strain Finegold B422
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