Difference between revisions of "ThiD"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=2I5B 2I5B] {{PubMed|16978644}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31620 O31620] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O31620 O31620] | ||
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<pubmed>19348578 </pubmed> | <pubmed>19348578 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>14973012,, </pubmed> | + | <pubmed>14973012,16978644 , </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:09, 3 February 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) |
| 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
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
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
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)
