Difference between revisions of "QueF"

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* '''Description:''' synthesis of the modified ribonukleotide queuosine <br/><br/>
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* '''Description:''' nitrile reductase (NADPH-dependent 7-cyano-7-deazaguanine reductase), synthesis of the modified ribonucleotide queuosine <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || unknown
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|style="background:#ABCDEF;" align="center"| '''Product''' || nitrile reductase
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || tRNA modification
 
|style="background:#ABCDEF;" align="center"|'''Function''' || tRNA modification
 +
|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU13750 queF]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 4.927   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 4.927   
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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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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13248&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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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]
 
|-
 
|-
 
|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>
 +
|-
 +
|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]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
  
 
<br/><br/>
 
<br/><br/>
 +
 +
= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[translation]]}}
 +
 +
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[preQ1 riboswitch]]}}
  
 
=The gene=
 
=The gene=
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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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=== Additional information===
 
=== Additional information===
 +
 +
  
  
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* '''Domains:'''  
 
* '''Domains:'''  
  
−
* '''Modification:'''
+
* '''Modification:''' active site Cys56 is S-bacillithiolated by NaOCl stress {{PubMed|22938038}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
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* '''Interactions:'''
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* '''[[SubtInteract|Interactions]]:'''
  
−
* '''Localization:''' cytoplasm (according to Swiss-Prot)
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* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13750&redirect=T BSU13750]
  
−
* '''Structure:'''
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* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=4F8b 4F8B] (covalent thioimide intermediate of the unimodular nitrile reductase [[QueF]]) {{PubMed|22787148}}
  
−
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O31678 O31678]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31678 O31678]
  
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13750]
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU13750]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/1.7.1.13 1.7.1.13]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/1.7.1.13 1.7.1.13]
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=Expression and regulation=
 
=Expression and regulation=
  
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* '''Operon:'''  
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* '''Operon:''' ''[[queC]]-[[queD]]-[[queE]]-[[queF]]'' {{PubMed|14660578}}
 +
 
 +
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=queF_1441291_1441788_1 queF] {{PubMed|22383849}}
  
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* '''[[Sigma factor]]:'''  
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* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
 +
** repressed in the presence of queuosine ([[preQ1 riboswitch]]) {{PubMed|19285444}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[preQ1 riboswitch]]: transcriptional antitermination in the absence of queuosine {{PubMed|19285444}}
  
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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 =
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=References=
 
=References=
  
−
<pubmed>14660578,, </pubmed>
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<pubmed>22938038,14660578,15767583 16511203 ,17929836 19285444 17384645 22787148 </pubmed>
 +
 
 +
[[Category:Protein-coding genes]]

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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