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RSAG_00645 protein (Ruminococcus sp. 5139BFAA) - STRING interaction network
"RSAG_00645" - Alanine racemase in Ruminococcus sp. 5139BFAA
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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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[Homology]
Score
RSAG_00645Alanine racemase ; Catalyzes the interconversion of L-alanine and D- alanine. May also act on other amino acids (381 aa)    
Predicted Functional Partners:
murF
D-alanyl-D-alanine-adding enzyme ; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein (456 aa)
   
  0.983
RSAG_01355
Uncharacterized protein (1517 aa)
     
 
  0.982
ddl
D-alanylalanine synthetase ; Cell wall formation (350 aa)
 
   
  0.950
RSAG_02370
UDP-N-acetylmuramyl-tripeptide synthetase (491 aa)
 
 
  0.861
RSAG_03249
Replicative DNA helicase ; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity (442 aa)
 
   
  0.816
RSAG_00646
Nicotinamide nucleotide repair protein ; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (499 aa)
   
   
  0.812
RSAG_03473
Uncharacterized protein (519 aa)
       
  0.785
murC
UDP-N-acetylmuramoyl-L-alanine synthetase ; Cell wall formation (467 aa)
 
  0.784
RSAG_03217
D-alanine-D-alanine ligase (331 aa)
       
  0.784
mraY
UDP-MurNAc-pentapeptide phosphotransferase ; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (322 aa)
   
  0.755
Your Current Organism:
Ruminococcus sp. 5139BFAA
NCBI taxonomy Id: 457412
Other names: R. sp. 5_1_39BFAA, Ruminococcus 5_1_39BFAA, Ruminococcus sp. 5139BFAA, Ruminococcus sp. 5_1_39BFAA
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