Difference between revisions of "CoaX"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2H3G 2H3G] (from ''Bacillus anthracis str. ames'', 75% identity, 88% similarity) {{PubMed|17323930}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37564 P37564] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37564 P37564] |
Revision as of 12:35, 18 February 2010
- Description: hypothetical protein
Gene name | coaX |
Synonyms | yacB |
Essential | no |
Product | pantothenate kinase (EC 2.7.1.33) |
Function | coenyzmeA synthesis |
Metabolic function and regulation of this protein in SubtiPathways: Coenzyme A | |
MW, pI | 26 kDa, 8.37 |
Gene length, protein length | 699 bp, 233 aa |
Immediate neighbours | ftsH, yacC |
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: BSU00700
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 + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate (according to Swiss-Prot)
- Protein family: type III pantothenate 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: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P37564
- KEGG entry: [2]
- E.C. number: 2.7.1.33
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
Leisl A Brand, Erick Strauss
Characterization of a new pantothenate kinase isoform from Helicobacter pylori.
J Biol Chem: 2005, 280(21);20185-8
[PubMed:15795230]
[WorldCat.org]
[DOI]
(P p)