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
AF_0386Orotate phosphoribosyl transferase, putative; Similar to GB:L77117 PID:1500547 percent identity: 39.04; identified by sequence similarity; putative; Belongs to the purine/pyrimidine phosphoribosyltransferase family. (195 aa)    
Predicted Functional Partners:
pyrD
Dihydroorotase dehydrogenase (pyrD); Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
  
  
 0.926
pyrF
Conserved hypothetical protein; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP); Belongs to the OMP decarboxylase family. Type 1 subfamily.
     
 0.916
pyrE
Orotate phosphoribosyl transferase (pyrE); Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
     
 0.916
pyrK
Cytochrome-c3 hydrogenase, subunit gamma; Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
     
  0.900
nob1
Conserved hypothetical protein; Toxic component of a type II toxin-antitoxin (TA) system. Processes pre-16S-rRNA at its 3' end (the D-site) to yield the mature 3' end (By similarity); Belongs to the PINc/VapC protein family.
 
     0.888
prs1
Ribose-phosphate pyrophosphokinase (prsA-1); 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).
    
  0.816
prs2
Ribose-phosphate pyrophosphokinase (prsA-2); 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).
    
  0.816
AF_0387
Glycosyltransferase, putative; Similar to PID:1652563 percent identity: 33.79; identified by sequence similarity; putative.
       0.813
AF_0388
Conserved hypothetical protein; Similar to GB:L77117 SP:Q58826 PID:1500312 percent identity: 40.13; identified by sequence similarity; putative.
       0.753
mqnA
Conserved hypothetical protein; Catalyzes the dehydration of chorismate into 3-[(1- carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
       0.753
Your Current Organism:
Archaeoglobus fulgidus
NCBI taxonomy Id: 224325
Other names: A. fulgidus DSM 4304, Archaeoglobus fulgidus DSM 4304, Archaeoglobus fulgidus VC-16, Archaeoglobus fulgidus str. DSM 4304, Archaeoglobus fulgidus strain DSM 4304
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.