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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ARA74979.1Aromatic alcohol reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (309 aa)    
Predicted Functional Partners:
nuoC
NADH-quinone oxidoreductase subunit 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 C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 0.993
ARA75754.1
NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 0.692
ARA75755.1
NADH-quinone oxidoreductase subunit 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.
   
 0.686
ARA75753.1
NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.671
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 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.
   
 0.662
ARA77067.1
Non-ribosomal peptide synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.595
ARA77674.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  0.581
ARA75052.1
Choline TMA-lyase-activating enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.574
ARA75496.1
Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.574
nuoI
NADH-quinone oxidoreductase subunit I; 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.
   
  0.574
Your Current Organism:
Pectobacterium brasiliense
NCBI taxonomy Id: 180957
Other names: CFBP 6617, Erwinia carotovora subsp. brasiliensis, LMG 21371, LMG:21371, NCPPB 4609, P. brasiliense, Pectobacterium brasiliense Portier et al. 2019, Pectobacterium brasiliensis, Pectobacterium carotovorum subsp. brasiliense, Pectobacterium carotovorum subsp. brasiliensis, strain 212
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