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
GDI0003Conserved hypothetical protein. (638 aa)    
Predicted Functional Partners:
nuoCD
Putative ADH-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.
     
 0.990
GDI0004
Conserved hypothetical protein.
 
    0.951
GDI3068
Putative ABC transporter.
    
 0.760
nuoG
Putative NADH-quinone oxidoreductase chain 3; Belongs to the complex I 75 kDa subunit family.
    
  0.736
nouG
NADH-quinone oxidoreductase chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.
    
  0.736
nouD
Putative NADH-ubiquinone oxidoreductase subunit 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; Belongs to the complex I 49 kDa subunit family.
     
 0.734
nouC
NADH-quinone oxidoreductase chain 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 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; Belongs to the complex I 30 kDa subunit family.
     
 0.734
nuoE
Putative NADH-quinone oxidoreductase chain E.
     
 0.713
nouE
NADH-quinone oxidoreductase chain E.
     
 0.713
nuoF
Putative NADH-quinone oxidoreductase chain F.
     
 0.709
Your Current Organism:
Gluconacetobacter diazotrophicus
NCBI taxonomy Id: 272568
Other names: G. diazotrophicus PA1 5, Gluconacetobacter diazotrophicus ATCC 49037, Gluconacetobacter diazotrophicus BR 11281, Gluconacetobacter diazotrophicus CCUG 37298, Gluconacetobacter diazotrophicus CIP 103539, Gluconacetobacter diazotrophicus DSM 5601, Gluconacetobacter diazotrophicus LMG 7603, Gluconacetobacter diazotrophicus NCCB 89154, Gluconacetobacter diazotrophicus PA1 5, Gluconacetobacter diazotrophicus str. PA1 5, Gluconacetobacter diazotrophicus strain PA1 5
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