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Mettu_1549 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1549" - Nicotinate-nucleotide pyrophosphorylase in Methylobacter tundripaludum
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second shell of interactors
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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]
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Mettu_1549Nicotinate-nucleotide pyrophosphorylase (276 aa)    
Predicted Functional Partners:
nadA
Quinolinate synthase A ; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (365 aa)
 
 
  0.999
nadD
Nicotinate mononucleotide adenylyltransferase ; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (210 aa)
       
  0.993
Mettu_0292
L-aspartate oxidase ; Catalyzes the oxidation of L-aspartate to iminoaspartate (531 aa)
   
  0.988
Mettu_0773
CinA domain protein (160 aa)
     
 
  0.889
Mettu_0269
Nicotinate phosphoribosyltransferase ; Catalyzes the synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP (443 aa)
   
  0.887
surE
Nucleoside 5’-monophosphate phosphohydrolase ; Nucleotidase that shows phosphatase activity on nucleoside 5’-monophosphates (251 aa)
     
 
    0.879
Mettu_1550
Putative uncharacterized protein (717 aa)
              0.865
Mettu_1548
Flavin reductase domain FMN-binding protein (159 aa)
              0.859
birA
Biotin-[acetyl-CoA carboxylase] synthetase ; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5’-adenylate (BirA-bio- 5’-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon (332 aa)
         
  0.829
Mettu_1551
N-acetylmuramyl-L-alanine amidase, negative regulator of AmpC, AmpD (180 aa)
         
  0.759
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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