close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
nnrEyjeF-like protein, hydroxyethylthiazole kinase-related protein; 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 d [...] (477 aa)    
Predicted Functional Partners:
moaC
Molybdenum cofactor biosynthesis protein MoaC; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family.
       0.799
nnrD
yjeF-like protein, hydroxyethylthiazole kinase-related protein; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S-and R-forms, the enzyme 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.
  
  
 
0.599
AFZ71602.1
Flavin-dependent dehydrogenase.
  
    0.459
AFZ72503.1
Nicotinamidase-like amidase; PFAM: Isochorismatase family.
 
    0.446
AFZ72436.1
PFAM: Pyridine nucleotide-disulphide oxidoreductase; NADH:flavin oxidoreductase / NADH oxidase family.
  
  
 0.430
folP-2
Dihydropteroate synthase; PFAM: Pterin binding enzyme; Mur ligase family, glutamate ligase domain; Mur ligase middle domain; TIGRFAM: dihydropteroate synthase; folylpolyglutamate synthase/dihydrofolate synthase.
  
    0.420
AFZ72672.1
Ammonia permease; PFAM: Ammonium Transporter Family; Nitrogen regulatory protein P-II; TIGRFAM: ammonium transporter; Belongs to the P(II) protein family.
       0.408
AFZ72001.1
NADH:ubiquinone oxidoreductase 49 kD subunit 7; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit.
       0.405
AFZ72105.1
NADH:ubiquinone oxidoreductase 49 kD subunit 7; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit.
       0.405
Your Current Organism:
Natronobacterium gregoryi
NCBI taxonomy Id: 797304
Other names: N. gregoryi SP2, Natronobacterium gregoryi ATCC 43098, Natronobacterium gregoryi JCM 8860, Natronobacterium gregoryi NCIMB 2189, Natronobacterium gregoryi SP2, Natronobacterium gregoryi str. SP2, Natronobacterium gregoryi strain SP2
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.