Difference between revisions of "ThyB"
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* '''Modification:''' | * '''Modification:''' | ||
+ | ** phosphorylated on Arg-102 {{PubMed|22517742}} | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
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=References= | =References= | ||
− | <pubmed> 19732150 2840350</pubmed> | + | <pubmed> 19732150 2840350 22517742</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:43, 21 April 2012
- Description: thymidylate synthase B
Gene name | thyB |
Synonyms | |
Essential | no |
Product | thymidylate synthase B |
Function | biosynthesis of thymidine nucleotides |
Interactions involving this protein in SubtInteract: ThyB | |
Metabolic function and regulation of this protein in SubtiPathways: Nucleotides (regulation) | |
MW, pI | 30 kDa, 6.272 |
Gene length, protein length | 792 bp, 264 aa |
Immediate neighbours | dfrA, ypjQ |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of nucleotides, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU21820
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- phosphorylated on Arg-102 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P11044
- KEGG entry: [2]
- E.C. number: 2.1.1.45
Additional information
Expression and regulation
- Sigma factor:
- 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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Rita A Eckart, Sabine Brantl, Andreas Licht
Search for additional targets of the transcriptional regulator CcpN from Bacillus subtilis.
FEMS Microbiol Lett: 2009, 299(2);223-31
[PubMed:19732150]
[WorldCat.org]
[DOI]
(I p)
M Iwakura, M Kawata, K Tsuda, T Tanaka
Nucleotide sequence of the thymidylate synthase B and dihydrofolate reductase genes contained in one Bacillus subtilis operon.
Gene: 1988, 64(1);9-20
[PubMed:2840350]
[WorldCat.org]
[DOI]
(P p)