STRINGSTRING
nadE nadE MJ_0917 MJ_0917 MJ_0541 MJ_0541 nadC nadC nadA nadA glnA glnA MJ_0670 MJ_0670 MJ_0806 MJ_0806 MJ_1619 MJ_1619 ribH ribH prs prs
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
nadENH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (259 aa)    
Predicted Functional Partners:
MJ_0917
Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...]
    
 0.971
MJ_0541
Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family.
    
 0.966
nadC
Nicotinate-nucleotide pyrophosphorylase (nadC); Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family.
     
 0.956
nadA
Quinolinate synthetase (nadA); Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
  
  
 0.942
glnA
Glutamine synthetase (glnA); Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate.
  
  
 0.698
MJ_0670
Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 37.37; identified by sequence similarity; putative.
 
  
 0.665
MJ_0806
X-pro aminopeptidase (pepQ); Similar to SP:P46545 PID:1150454 PID:609078 percent identity: 33.33; identified by sequence similarity; putative.
 
    0.612
MJ_1619
Biotin operon repressor/biotin--[acetyl-CoA-carboxylase] ligase (birA); Similar to GB:L42023 SP:P46363 PID:1161402 PID:1222142 PID:1204478 percent identity: 29.41; identified by sequence similarity; putative.
  
  
 0.591
ribH
Riboflavin synthase beta chain (ribH); Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family.
     
 0.582
prs
Ribose-phosphate pyrophosphokinase, (prsA); Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P). It can also use dATP as diphosphoryl donor.
     
 0.578
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.