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
ribH6,7-dimethyl-8-ribityllumazine synthase; 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. (161 aa)    
Predicted Functional Partners:
ALM10643.1
Riboflavin synthase.
 
 0.999
ribBA
GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
  
 
 0.999
ALM10759.1
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
 
 0.999
ALM11013.1
Riboflavin biosynthesis protein RibF.
  
 
 0.933
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
 
 0.818
nusB
Transcription termination protein NusB; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
  
  
 0.719
pyrB
Aspartate carbamoyltransferase catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
  
    0.613
rplU
Large subunit ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
   
    0.603
uvrA
Excinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
       0.563
ALM10645.1
Cell wall hydrolase/autolysin.
       0.526
Your Current Organism:
Peribacter riflensis
NCBI taxonomy Id: 1735162
Other names: C. Peribacter riflensis, Candidatus Peregrinibacteria bacterium RIFOXYA2_FULL_PER-ii_58_14, Candidatus Peregrinibacteria bacterium RIFOXYB2_FULL_PER-ii_58_17, Candidatus Peregrinibacteria bacterium RIFOXYC2_FULL_PER-ii_58_32, Candidatus Peregrinibacteria bacterium RIFOXYD1_FULL_PER-ii_59_16, Candidatus Peregrinibacteria bacterium RIFOXYD2_FULL_PER-ii_51_23, Candidatus Peribacter riflensis, Candidatus Peribacteria bacterium RIFOXYA2_FULL_PER-ii_58_14, Candidatus Peribacteria bacterium RIFOXYB2_FULL_PER-ii_58_17, Candidatus Peribacteria bacterium RIFOXYC2_FULL_PER-ii_58_32, Candidatus Peribacteria bacterium RIFOXYD1_FULL_PER-ii_59_16, Candidatus Peribacteria bacterium RIFOXYD2_FULL_PER-ii_51_23
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.