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
nnrNAD(P)H-hydrate epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of bot [...] (511 aa)    
Predicted Functional Partners:
hepA
Endonuclease.
  
 0.954
ARP42701.1
RNA pyrophosphohydrolase; Belongs to the Nudix hydrolase family.
  
 0.950
nudK
GDP-mannose pyrophosphatase NudK.
  
 0.950
nudF
ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family.
  
 0.950
cshA_1
DEAD-box ATP-dependent RNA helicase CshA; Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
  
 0.923
cshA_2
DEAD-box ATP-dependent RNA helicase CshA; DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity; Belongs to the DEAD box helicase family. CshA subfamily.
  
 0.923
nuoD
NADH-quinone 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 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 49 kDa subunit family.
  
 
 0.809
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.
  
   0.774
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
   0.755
tsaE
tRNA threonylcarbamoyladenosine biosynthesis protein TsaE.
  
 
 0.727
Your Current Organism:
Geobacillus thermodenitrificans
NCBI taxonomy Id: 33940
Other names: ATCC 29492, BGSC 94A1, Bacillus sp. BGSC W9A21, Bacillus sp. BGSC W9A45, Bacillus sp. BGSC W9A5, Bacillus sp. BGSC W9A54, Bacillus sp. BGSC W9A65, Bacillus sp. BGSC W9A66, Bacillus sp. BGSC W9A67, Bacillus sp. BGSC W9A69, Bacillus sp. BGSC W9A71, Bacillus sp. BGSC W9A73, Bacillus sp. BGSC W9A74, Bacillus sp. BGSC W9A86, Bacillus sp. BGSC W9A87, Bacillus sp. BGSC W9A91, Bacillus thermodenitrificans, DSM 465, G. thermodenitrificans, Geobacillus sp. A333, Geobacillus sp. F84a, Geobacillus sp. G11MC16, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Cihan et al. 2011, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Coorevits et al. 2012, LMG 17532, LMG:17532, strain R-35647
Server load: low (24%) [HD]