Difference between revisions of "QueA"
| Line 30: | Line 30: | ||
<br/><br/> | <br/><br/> | ||
| + | |||
| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[translation]]}} | ||
| + | |||
| + | = This gene is a member of the following [[regulons]] = | ||
| + | |||
=The gene= | =The gene= | ||
| Line 49: | Line 55: | ||
| − | + | ||
| − | |||
=The protein= | =The protein= | ||
Revision as of 21:55, 8 December 2010
- Description: S-adenosylmethionine tRNA ribosyltransferase
| Gene name | queA |
| Synonyms | |
| Essential | no |
| Product | S-adenosylmethionine tRNA ribosyltransferase |
| Function | tRNA modification |
| MW, pI | 38 kDa, 5.047 |
| Gene length, protein length | 1026 bp, 342 aa |
| Immediate neighbours | tgt, ruvB |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
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
- 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:
- Interactions:
- Localization:
Database entries
- Structure: 1YY3
- UniProt: O32054
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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)
