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
SKA75123.1Nickel-dependent hydrogenase; Belongs to the complex I 49 kDa subunit family. (358 aa)    
Predicted Functional Partners:
SKA75145.1
Ech hydrogenase subunit C; Belongs to the complex I 20 kDa subunit family.
 0.997
SKA75150.1
Ech hydrogenase subunit B.
 
 0.990
SKA67826.1
Ni,Fe-hydrogenase III small subunit.
 0.985
SKA68109.1
Ni,Fe-hydrogenase III small subunit.
 0.985
SKA75115.1
Ech hydrogenase subunit F.
 
 0.960
SKA75139.1
Respiratory-chain NADH dehydrogenase, subunit.
 
 
 0.960
SKA67830.1
NADH-quinone oxidoreductase subunit H.
 
 0.953
SKA68105.1
NADH-quinone oxidoreductase subunit H.
 
 0.953
SKA75154.1
Ech hydrogenase subunit A.
 
   
 0.934
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.
     0.832
Your Current Organism:
Desulfovibrio bizertensis
NCBI taxonomy Id: 1121442
Other names: D. bizertensis DSM 18034, Desulfovibrio bizertensis DSM 18034
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