Difference between revisions of "ThiL"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1VQV 1VQV] (from ''Aquifex aeolicus'', 33% similarity, 51% identity) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O05514 O05514] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O05514 O05514] |
Revision as of 16:13, 3 February 2010
- Description: thiamine-monophosphate kinase
Gene name | thiL |
Synonyms | ydiA, ydxA |
Essential | no |
Product | thiamine-monophosphate kinase |
Function | biosynthesis of thiamine |
MW, pI | 35 kDa, 5.036 |
Gene length, protein length | 975 bp, 325 aa |
Immediate neighbours | trnE-Asp, ydiB |
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: BSU05900
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + thiamine phosphate = ADP + thiamine diphosphate (according to Swiss-Prot)
- Protein family: thiamine-monophosphate kinase 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: 1VQV (from Aquifex aeolicus, 33% similarity, 51% identity)
- UniProt: O05514
- KEGG entry: [2]
- E.C. number: 2.7.4.16
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
Reviews
Original publications
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)