Difference between revisions of "QueA"

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Revision as of 10:02, 20 April 2012

  • Description: S-adenosylmethionine tRNA ribosyltransferase

Gene name queA
Synonyms
Essential no
Product S-adenosylmethionine tRNA ribosyltransferase
Function tRNA modification
MW, pI 38 kDa, 5.047
Gene length, protein length 1026 bp, 342 aa
Immediate neighbours tgt, ruvB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
QueA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
QueA expression.png
























Categories containing this gene/protein

translation

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU27720

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: S-adenosylmethionine + 7-aminomethyl-7-deazaguanosine = methionine + adenine + epoxyqueuosine (according to Swiss-Prot)
  • Protein family: queA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Clemens Grimm, Ralf Ficner, Tanja Sgraja, Peter Haebel, Gerhard Klebe, Klaus Reuter
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase.
Biochem Biophys Res Commun: 2006, 351(3);695-701
[PubMed:17083917] [WorldCat.org] [DOI] (P p)

C Grimm, G Klebe, R Ficner, K Reuter
Screening orthologs as an important variable in crystallization: preliminary X-ray diffraction studies of the tRNA-modifying enzyme S-adenosyl-methionine:tRNA ribosyl transferase/isomerase.
Acta Crystallogr D Biol Crystallogr: 2000, 56(Pt 4);484-8
[PubMed:10739928] [WorldCat.org] [DOI] (P p)