Difference between revisions of "QueF"
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− | * '''Description:''' nitrile reductase, synthesis of the modified | + | * '''Description:''' nitrile reductase, synthesis of the modified ribonucleotide queuosine <br/><br/> |
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''[[queC]]-[[queD]]-[[queE]]-[[queF]]'' {{PubMed|14660578}} |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' |
Revision as of 20:03, 3 October 2009
- Description: nitrile reductase, synthesis of the modified ribonucleotide queuosine
Gene name | queF |
Synonyms | ykvM |
Essential | no |
Product | nitrile reductase |
Function | tRNA modification |
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 This image was kindly provided by SubtiList
|
Contents
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:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O31678
- KEGG entry: [2]
- E.C. number: 1.7.1.13
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- 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
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)
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)