QueF

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  • Description: nitrile reductase (NADPH-dependent 7-cyano-7-deazaguanine reductase), synthesis of the modified ribonucleotide queuosine

Gene name queF
Synonyms ykvM
Essential no
Product nitrile reductase
Function tRNA modification
Gene expression levels in SubtiExpress: queF
MW, pI 19 kDa, 4.927
Gene length, protein length 495 bp, 165 aa
Immediate neighbours queE, ykvN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YkvM context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
QueF expression.png
























Categories containing this gene/protein

translation

This gene is a member of the following regulons

preQ1 riboswitch

The gene

Basic information

  • Locus tag: BSU13750

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2 NADPH (according to Swiss-Prot)
  • Protein family: QueF type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: active site Cys56 is S-bacillithiolated by NaOCl stress PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 4F8B (covalent thioimide intermediate of the unimodular nitrile reductase QueF) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Sigma factor:
  • 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

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

Vimbai M Chikwana, Boguslaw Stec, Bobby W K Lee, Valérie de Crécy-Lagard, Dirk Iwata-Reuyl, Manal A Swairjo
Structural basis of biological nitrile reduction.
J Biol Chem: 2012, 287(36);30560-70
[PubMed:22787148] [WorldCat.org] [DOI] (I p)

Mijeong Kang, Robert Peterson, Juli Feigon
Structural Insights into riboswitch control of the biosynthesis of queuosine, a modified nucleotide found in the anticodon of tRNA.
Mol Cell: 2009, 33(6);784-90
[PubMed:19285444] [WorldCat.org] [DOI] (I p)

Bobby W K Lee, Steven G Van Lanen, Dirk Iwata-Reuyl
Mechanistic studies of Bacillus subtilis QueF, the nitrile oxidoreductase involved in queuosine biosynthesis.
Biochemistry: 2007, 46(44);12844-54
[PubMed:17929836] [WorldCat.org] [DOI] (P p)

Adam Roth, Wade C Winkler, Elizabeth E Regulski, Bobby W K Lee, Jinsoo Lim, Inbal Jona, Jeffrey E Barrick, Ankita Ritwik, Jane N Kim, Rüdiger Welz, Dirk Iwata-Reuyl, Ronald R Breaker
A riboswitch selective for the queuosine precursor preQ1 contains an unusually small aptamer domain.
Nat Struct Mol Biol: 2007, 14(4);308-17
[PubMed:17384645] [WorldCat.org] [DOI] (P p)

Manal A Swairjo, Robert R Reddy, Bobby Lee, Steven G Van Lanen, Shannon Brown, Valérie de Crécy-Lagard, Dirk Iwata-Reuyl, Paul Schimmel
Crystallization and preliminary X-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2005, 61(Pt 10);945-8
[PubMed:16511203] [WorldCat.org] [DOI] (I p)

Steven G Van Lanen, John S Reader, Manal A Swairjo, Valérie de Crécy-Lagard, Bobby Lee, Dirk Iwata-Reuyl
From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold.
Proc Natl Acad Sci U S A: 2005, 102(12);4264-9
[PubMed:15767583] [WorldCat.org] [DOI] (P p)

John S Reader, David Metzgar, Paul Schimmel, Valérie de Crécy-Lagard
Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine.
J Biol Chem: 2004, 279(8);6280-5
[PubMed:14660578] [WorldCat.org] [DOI] (P p)