QueE

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  • Description: 7-carboxy-7-deazaguanine (CDG) synthase, required for the synthesis of the modified ribonucleotide queuosine

Gene name queE
Synonyms ykvL
Essential no
Product 7-carboxy-7-deazaguanine (CDG) synthase
Function tRNA modification
Gene expression levels in SubtiExpress: queE
Interactions involving this protein in SubtInteract: QueE
MW, pI 26 kDa, 4.962
Gene length, protein length 729 bp, 243 aa
Immediate neighbours queD, queF
Sequences Protein DNA DNA_with_flanks
Genetic context
YkvL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
QueE 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: BSU13740

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

    • conversion of 6-carboxy-5,6,7,8-tetrahydropterin to 7-carboxy-7-deazaguanine (CDG) PubMed
  • Catalyzed reaction/ biological activity:
  • Protein family: radical S-adenosyl-L-methionine (SAM) superfamily
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): [4Fe-4S] cluster, S-adenosyl-L-methionine, Mg(2+) PubMed
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Nathan A Bruender, Anthony P Young, Vahe Bandarian
Chemical and Biological Reduction of the Radical SAM Enzyme 7-Carboxy-7-deazaguanine [corrected] Synthase.
Biochemistry: 2015, 54(18);2903-10
[PubMed:25933252] [WorldCat.org] [DOI] (I p)

Daniel P Dowling, Nathan A Bruender, Anthony P Young, Reid M McCarty, Vahe Bandarian, Catherine L Drennan
Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.
Nat. Chem. Biol.: 2014, 10(2);106-12
[PubMed:24362703] [WorldCat.org] [DOI] (I p)

Reid M McCarty, Carsten Krebs, Vahe Bandarian
Spectroscopic, steady-state kinetic, and mechanistic characterization of the radical SAM enzyme QueE, which catalyzes a complex cyclization reaction in the biosynthesis of 7-deazapurines.
Biochemistry: 2013, 52(1);188-98
[PubMed:23194065] [WorldCat.org] [DOI] (I p)

Reid M McCarty, Arpád Somogyi, Guangxin Lin, Neil E Jacobsen, Vahe Bandarian
The deazapurine biosynthetic pathway revealed: in vitro enzymatic synthesis of PreQ(0) from guanosine 5'-triphosphate in four steps.
Biochemistry: 2009, 48(18);3847-52
[PubMed:19354300] [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)

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)

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)