QueA

• Description: S-adenosylmethionine tRNA ribosyltransferase
  
  

Gene name	queA
Synonyms
Essential	no
Product	S-adenosylmethionine tRNA ribosyltransferase
Function	tRNA modification
Gene expression levels in SubtiExpress: queA
MW, pI	38 kDa, 5.047
Gene length, protein length	1026 bp, 342 aa
Immediate neighbours	tgt, yrzS
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation

The gene

Basic information

• Locus tag: BSU27720

Database entries

• BsubCyc: BSU27720

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU27720

• Structure: 1YY3

• UniProt: O32054

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: queA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 154 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 395 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)