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cmoA protein (Methylobacter tundripaludum) - STRING interaction network
"cmoA" - Carboxy-S-adenosyl-L-methionine synthase in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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cmoACarboxy-S-adenosyl-L-methionine synthase ; Catalyzes the conversion of 5-methoxyuridine (mo5U) to uridine-5-oxyacetic acid (cmo5U) at position 34 in tRNA. May also participate in the methylation of uridine-5-oxyacetic acid (cmo5U) to uridine-5-oxyacetic acid methyl ester (mcmo5U) (243 aa)    
Predicted Functional Partners:
cmoB
tRNA U34 carboxymethyltransferase ; Catalyzes carboxymethyl transfer from carboxy-S- adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs (324 aa)
 
 
  0.996
nuoC
NDH-1 subunit C/D ; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (592 aa)
     
  0.887
gcvP
Glycine dehydrogenase (aminomethyl-transferring) ; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (963 aa)
     
 
    0.882
Mettu_2353
tRNA m6A37 methyltransferase ; Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC) (242 aa)
 
  0.815
thiG
Thiazole synthase ; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5- phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S (325 aa)
       
  0.793
bioB
Biotin synthase ; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical- based mechanism (322 aa)
   
 
  0.772
Mettu_4177
8-amino-7-oxononanoate synthase (407 aa)
   
 
  0.765
Mettu_3064
8-amino-7-oxononanoate synthase (414 aa)
   
 
  0.765
bioF
8-amino-7-ketopelargonate synthase ; Catalyzes the decarboxylative condensation of pimeloyl- [acyl-carrier protein] and L-alanine to produce 8-amino-7- oxononanoate (AON), [acyl-carrier protein], and carbon dioxide (389 aa)
   
 
  0.765
bioD
Dethiobiotin synthase ; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring (219 aa)
   
 
  0.749
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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