Difference between revisions of "ThiD"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[biosynthesis of cofactors]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[Thi-box]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 18:33, 8 December 2010
- Description: 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase
| Gene name | thiD |
| Synonyms | yjbV |
| Essential | no |
| Product | 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase |
| Function | biosynthesis of thiamine pyrophosphate (TPP) |
| Metabolic function and regulation of this protein in SubtiPathways: Thiamin | |
| MW, pI | 28 kDa, 5.709 |
| Gene length, protein length | 813 bp, 271 aa |
| Immediate neighbours | thiF, fabI |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU11710
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s): PdxK
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: O31620
- KEGG entry: [3]
Additional information
Expression and 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
Joseph A Newman, Sanjan K Das, Svetlana E Sedelnikova, David W Rice
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parallel emergence of enzyme activity during evolution.
J Mol Biol: 2006, 363(2);520-30
[PubMed:16978644]
[WorldCat.org]
[DOI]
(P p)
Joo-Heon Park, Kristin Burns, Cynthia Kinsland, Tadhg P Begley
Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase.
J Bacteriol: 2004, 186(5);1571-3
[PubMed:14973012]
[WorldCat.org]
[DOI]
(P p)
