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.
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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
ANN79558.1Alpha/beta hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (275 aa)    
Predicted Functional Partners:
ANN76991.1
NADH oxidoreductase (quinone) 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.
   
 
 0.674
ANN79432.1
Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.674
ANN76990.1
NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.643
ANN79431.1
Formate dehydrogenase subunit gamma; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.643
nuoD
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; Belongs to the complex I 49 kDa subunit family.
   
 
 0.625
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 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
ANN79557.1
LysR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LysR transcriptional regulatory family.
       0.550
nuoC
NADH-quinone oxidoreductase subunit 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.
   
 
 0.534
ANN76203.1
Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.514
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.
   
   0.514
Your Current Organism:
Bordetella flabilis
NCBI taxonomy Id: 463014
Other names: B. flabilis, Bordetella flabilis Vandamme et al. 2015, Bordetella sp. AU10664, CCUG 56827, LMG 28642, LMG:28642, strain AU10664
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