ThiL

• Description: thiamine-monophosphate kinase
  
  

Gene name	thiL
Synonyms	ydiA, ydxA
Essential	no
Product	thiamine-monophosphate kinase
Function	biosynthesis of thiamine
Metabolic function and regulation of this protein in SubtiPathways: Thiamin synthesis
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

The gene

Basic information

• Locus tag: BSU05900

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

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)