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
EHH01717.14Fe-4S binding domain protein; KEGG: bvu:BVU_2314 1.8e-28 hypothetical protein; K00176 2-oxoglutarate ferredoxin oxidoreductase subunit delta. (76 aa)    
Predicted Functional Partners:
nuoD
Respiratory-chain NADH dehydrogenase, subunit; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
 0.999
EHH01718.1
KEGG: pmz:HMPREF0659_A5966 1.2e-150 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) K00174; Psort location: Cytoplasmic, score: 8.96.
 
 0.995
EHH01720.1
Thiamine pyrophosphate enzyme, TPP binding domain protein; KEGG: bfs:BF1653 1.5e-118 putative 2-oxoglutarate synthase subunit; K00175 2-oxoglutarate ferredoxin oxidoreductase subunit beta.
 
 0.994
EHH01721.1
2-oxoacid:ferredoxin/flavodoxin oxidoreductase, gamma subunit; KEGG: bfr:BF1645 2.0e-75 ketoisovalerate oxidoreductase subunit VorA; K00177 2-oxoglutarate ferredoxin oxidoreductase subunit gamma.
 
  0.994
EHH00630.1
KEGG: bvu:BVU_3787 0. pyruvate-flavodoxin oxidoreductase; K03737 putative pyruvate-flavodoxin oxidoreductase; Psort location: Cytoplasmic, score: 8.96.
  
 0.971
EHH01168.1
2-oxoacid:acceptor oxidoreductase, alpha subunit; KEGG: bvu:BVU_0979 5.4e-288 2-oxoglutarate synthase subunit KorA; K00174 2-oxoglutarate ferredoxin oxidoreductase subunit alpha; Psort location: Cytoplasmic, score: 8.96.
  
 0.956
nuoB
NADH-quinone oxidoreductase subunit B; 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.
  
 0.941
nuoH
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 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.
  
 0.926
EHH00898.1
Proton-translocating NADH-quinone oxidoreductase, chain M; KEGG: bvu:BVU_1751 7.7e-225 NADH dehydrogenase I chain M; K00342 NADH dehydrogenase I subunit M; Psort location: CytoplasmicMembrane, score: 10.00.
  
 0.925
nuoA
Putative NADH dehydrogenase 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.
  
 0.921
Your Current Organism:
Paraprevotella clara
NCBI taxonomy Id: 762968
Other names: P. clara YIT 11840, Paraprevotella clara YIT 11840, Paraprevotella clara str. YIT 11840, Paraprevotella clara strain YIT 11840
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