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
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
prsRibose-phosphate pyrophosphokinase; 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); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily. (334 aa)    
Predicted Functional Partners:
glmU
UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain.
  
 0.991
ACV06847.1
2-oxoglutarate dehydrogenase E1 component; PFAM: Transketolase, pyrimidine binding domain; 2-oxoacid dehydrogenases acyltransferase (catalytic domain); Dehydrogenase E1 component; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 component.
  
 0.968
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
  
 0.950
ACV06352.1
PFAM: Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain; Transketolase, thiamine diphosphate binding domain; TIGRFAM: transketolase, bacterial and yeast; Belongs to the transketolase family.
   
 
 0.942
ACV05952.1
PFAM: Ribose/Galactose Isomerase; TIGRFAM: sugar-phosphate isomerases, RpiB/LacA/LacB family; ribose 5-phosphate isomerase.
    
 0.924
ACV05321.1
Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit; PFAM: Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain.
   
 0.894
ACV05526.1
Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit; PFAM: Transketolase, pyrimidine binding domain; Transketolase, C-terminal domain.
   
 0.894
pyrE
Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
  
 
 0.853
rplY
LSU ribosomal protein L25P; This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
  
  
 0.852
hisG
ATP phosphoribosyltransferase (homohexameric); Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
  
 
 0.852
Your Current Organism:
Kytococcus sedentarius
NCBI taxonomy Id: 478801
Other names: K. sedentarius DSM 20547, Kytococcus sedentarius DSM 20547, Kytococcus sedentarius str. DSM 20547, Kytococcus sedentarius strain DSM 20547
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.