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
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[Homology]
Score
prsAPhosphoribosyl pyrophosphate synthetase; 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. (339 aa)    
Predicted Functional Partners:
glmU
Glucosamine-1-phosphate N-acetyltransferase; 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. In the C-terminal section; belongs to the transferase hexapeptide repeat family.
  
 0.990
pdhAb
Dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
  
 0.988
RSP_1294
IMG reference gene:2512956340; PFAM: Dehydrogenase E1 component; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain.
  
 0.975
tktA
Transketolase; IMG reference gene:2512954921; PFAM: Transketolase, thiamine diphosphate binding domain; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain; TIGRFAM: transketolase, bacterial and yeast; Belongs to the transketolase family.
   
 
 0.952
tklB
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
   
 
 0.950
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
  
 0.942
cbbI
Ribose-5-phosphate isomerase; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
  
 
 0.933
rbsK
Putative RbsK, Carbohydrate kinase, ribokinase family; Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
  
 0.924
deoB
Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family.
     
 0.924
rbsK-2
Carbohydrate kinase, PfkB/Ribokinase; Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
   
 0.924
Your Current Organism:
Rhodobacter sphaeroides 241
NCBI taxonomy Id: 272943
Other names: R. sphaeroides 2.4.1, Rhodobacter sphaeroides 2.4.1, Rhodobacter sphaeroides ATCC 17023, Rhodobacter sphaeroides ATH 2.4.1, Rhodobacter sphaeroides str. 2.4.1, Rhodobacter sphaeroides strain 2.4.1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.