Difference between revisions of "RibC"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:36, 6 December 2013
- Description: riboflavin kinase / FAD synthase
Gene name | ribC |
Synonyms | |
Essential | yes PubMed |
Product | riboflavin kinase / FAD synthase |
Function | FAD biosynthesis |
Gene expression levels in SubtiExpress: ribC | |
Metabolic function and regulation of this protein in SubtiPathways: Riboflavin / FAD | |
MW, pI | 35 kDa, 8.3 |
Gene length, protein length | 948 bp, 316 aa |
Immediate neighbours | truB, rpsO |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis of cofactors, essential genes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU16670
Phenotypes of a mutant
- essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + riboflavin = ADP + FMN (according to Swiss-Prot)
- Protein family: ribF family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P54575
- KEGG entry: [2]
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
Kosei Tanaka, Christopher S Henry, Jenifer F Zinner, Edmond Jolivet, Matthew P Cohoon, Fangfang Xia, Vladimir Bidnenko, S Dusko Ehrlich, Rick L Stevens, Philippe Noirot
Building the repertoire of dispensable chromosome regions in Bacillus subtilis entails major refinement of cognate large-scale metabolic model.
Nucleic Acids Res: 2013, 41(1);687-99
[PubMed:23109554]
[WorldCat.org]
[DOI]
(I p)
Weiru Wang, Rosalind Kim, Hisao Yokota, Sung-Hou Kim
Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima.
Proteins: 2005, 58(1);246-8
[PubMed:15468322]
[WorldCat.org]
[DOI]
(I p)
M Mack, A P van Loon, H P Hohmann
Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC.
J Bacteriol: 1998, 180(4);950-5
[PubMed:9473052]
[WorldCat.org]
[DOI]
(P p)