Difference between revisions of "ThiC"
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==Original publications== | ==Original publications== | ||
<pubmed>16291685 9370266 20509597 12376536</pubmed> | <pubmed>16291685 9370266 20509597 12376536</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:18, 11 August 2010
- Description: biosynthesis of the pyrimidine moiety of thiamine
Gene name | thiC |
Synonyms | thiA |
Essential | no |
Product | unknown |
Function | biosynthesis of thiamine |
Metabolic function and regulation of this protein in SubtiPathways: Thiamin | |
MW, pI | 65 kDa, 5.262 |
Gene length, protein length | 1770 bp, 590 aa |
Immediate neighbours | ygaJ, ygaK |
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: BSU08790
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: thiC family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated on Ser-565, Ser-586 and Tyr-589 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1G6C
- UniProt: P45740
- KEGG entry: [2]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Christopher T Jurgenson, Tadhg P Begley, Steven E Ealick
The structural and biochemical foundations of thiamin biosynthesis.
Annu Rev Biochem: 2009, 78;569-603
[PubMed:19348578]
[WorldCat.org]
[DOI]
(I p)
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
Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597]
[WorldCat.org]
[DOI]
(I p)
Ghislain Schyns, Sébastien Potot, Yi Geng, Teresa M Barbosa, Adriano Henriques, John B Perkins
Isolation and characterization of new thiamine-deregulated mutants of Bacillus subtilis.
J Bacteriol: 2005, 187(23);8127-36
[PubMed:16291685]
[WorldCat.org]
[DOI]
(P p)
Dmitry A Rodionov, Alexey G Vitreschak, Andrey A Mironov, Mikhail S Gelfand
Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms.
J Biol Chem: 2002, 277(50);48949-59
[PubMed:12376536]
[WorldCat.org]
[DOI]
(P p)
Y Zhang, T P Begley
Cloning, sequencing and regulation of thiA, a thiamin biosynthesis gene from Bacillus subtilis.
Gene: 1997, 198(1-2);73-82
[PubMed:9370266]
[WorldCat.org]
[DOI]
(P p)