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ribC protein (Synechocystis sp. PCC6803) - STRING interaction network
"ribC" - Riboflavin synthase alpha chain in Synechocystis sp. PCC6803
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second shell of interactors
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proteins of unknown 3D structure
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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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ribCRiboflavin synthase alpha chain (226 aa)    
Predicted Functional Partners:
ribH
Riboflavin synthase beta subunit; 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 (164 aa)
 
  0.998
ribBA
GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate (556 aa)
 
  0.997
ribD
Riboflavin biosynthesis protein; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate (368 aa)
 
  0.986
ribF
Bifunctional riboflavin kinase/FMN adenylyltransferase (313 aa)
   
  0.985
slr0326
Hypothetical protein (147 aa)
              0.653
smpB
Small protein; Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a ’tag peptide’, a short internal open reading frame. During trans-translation Ala- aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to transl [...] (154 aa)
       
    0.594
hisI
phosphoribosyl-ATP pyrophosphohydrolase (215 aa)
   
   
  0.540
hitB
Iron utilization protein (557 aa)
              0.503
thiL
Thiamine monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1 (364 aa)
 
        0.498
nusB
N utilization substance protein B; Involved in the transcription termination process (221 aa)
   
   
  0.492
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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