Difference between revisions of "TenA"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 07:45, 8 December 2013
- Description: thiaminase II
Gene name | tenA |
Synonyms | |
Essential | no |
Product | thiaminase II |
Function | thiamine salvage |
Gene expression levels in SubtiExpress: tenA | |
Metabolic function and regulation of this protein in SubtiPathways: Thiamin | |
MW, pI | 27 kDa, 4.99 |
Gene length, protein length | 708 bp, 236 aa |
Immediate neighbours | yjbQ, tenI |
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: BSU11650
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole (according to Swiss-Prot)
- Protein family: thiaminase-2 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
- UniProt: P25052
- KEGG entry: [3]
- E.C. number: 3.5.99.2
Additional information
Expression and regulation
- Sigma factor:
- 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
Reviews
T P Begley, D M Downs, S E Ealick, F W McLafferty, A P Van Loon, S Taylor, N Campobasso, H J Chiu, C Kinsland, J J Reddick, J Xi
Thiamin biosynthesis in prokaryotes.
Arch Microbiol: 1999, 171(5);293-300
[PubMed:10382260]
[WorldCat.org]
[DOI]
(P p)
Original publications
Afshan Begum, Julia Drebes, Alexey Kikhney, Ingrid B Müller, Markus Perbandt, Dmitri Svergun, Carsten Wrenger, Christian Betzel
Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases.
Acta Crystallogr D Biol Crystallogr: 2013, 69(Pt 12);2320-9
[PubMed:24311574]
[WorldCat.org]
[DOI]
(I p)
Amy L Jenkins, Yang Zhang, Steven E Ealick, Tadhg P Begley
Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.
Bioorg Chem: 2008, 36(1);29-32
[PubMed:18054064]
[WorldCat.org]
[DOI]
(I p)
Amy Haas Jenkins, Ghislain Schyns, Sébastien Potot, Guangxing Sun, Tadhg P Begley
A new thiamin salvage pathway.
Nat Chem Biol: 2007, 3(8);492-7
[PubMed:17618314]
[WorldCat.org]
[DOI]
(P p)
Narasimhan Sudarsan, Smadar Cohen-Chalamish, Shingo Nakamura, Gail Mitchell Emilsson, Ronald R Breaker
Thiamine pyrophosphate riboswitches are targets for the antimicrobial compound pyrithiamine.
Chem Biol: 2005, 12(12);1325-35
[PubMed:16356850]
[WorldCat.org]
[DOI]
(P p)
Angela V Toms, Amy L Haas, Joo-Heon Park, Tadhg P Begley, Steven E Ealick
Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II.
Biochemistry: 2005, 44(7);2319-29
[PubMed:15709744]
[WorldCat.org]
[DOI]
(P p)