Difference between revisions of "QueF"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[queE]]'', ''[[ykvN]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[queE]]'', ''[[ykvN]]''
 
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|-
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13750 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13750 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13750 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13750 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13750 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13750 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ykvM_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ykvM_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=queF_1441291_1441788_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:queF_expression.png|500px]]
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=queF_1441291_1441788_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:queF_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU13750]]
 
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13750&redirect=T BSU13750]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13750&redirect=T BSU13750]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=4F8b 4F8B] (covalent thioimide intermediate of the unimodular nitrile reductase [[QueF]]) {{PubMed|22787148}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=4F8b 4F8B] (covalent thioimide intermediate of the unimodular nitrile reductase [[QueF]]) {{PubMed|22787148}}
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* '''Additional information:'''
 
* '''Additional information:'''
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 303 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 913 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Latest revision as of 09:43, 17 April 2014

  • 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
Sequences Protein DNA DNA_with_flanks
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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 303 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 913 PubMed

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)

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