QueA
Revision as of 14:23, 2 April 2014 by 134.76.38.147 (talk)
-  Description: S-adenosylmethionine tRNA ribosyltransferase 
| Gene name | queA | 
| Synonyms | |
| Essential | no | 
| Product | S-adenosylmethionine tRNA ribosyltransferase | 
| Function | tRNA modification | 
| Gene expression levels in SubtiExpress: queA | |
| MW, pI | 38 kDa, 5.047 | 
| Gene length, protein length | 1026 bp, 342 aa | 
| Immediate neighbours | tgt, yrzS | 
| Sequences | Protein DNA DNA_with_flanks | 
| Genetic context    This image was kindly provided by SubtiList | |
| Expression at a glance   PubMed   | |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27720
Phenotypes of a mutant
Database entries
- BsubCyc: BSU27720
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: S-adenosylmethionine + 7-aminomethyl-7-deazaguanosine = methionine + adenine + epoxyqueuosine (according to Swiss-Prot)
- Protein family: queA family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU27720
- Structure: 1YY3
- UniProt: O32054
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
Clemens Grimm, Ralf Ficner, Tanja Sgraja, Peter Haebel, Gerhard Klebe, Klaus Reuter  
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase. 
Biochem Biophys Res Commun: 2006, 351(3);695-701 
[PubMed:17083917]
  [WorldCat.org]
 [DOI]
 (P p)
C Grimm, G Klebe, R Ficner, K Reuter  
Screening orthologs as an important variable in crystallization: preliminary X-ray diffraction studies of the tRNA-modifying enzyme S-adenosyl-methionine:tRNA ribosyl transferase/isomerase. 
Acta Crystallogr D Biol Crystallogr: 2000, 56(Pt 4);484-8 
[PubMed:10739928]
  [WorldCat.org]
 [DOI]
 (P p)

