Difference between revisions of "RibC"
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|style="background:#ABCDEF;" align="center"|'''Function''' || FAD biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || FAD biosynthesis | ||
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+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/riboflavin.html Riboflavin and FAD synthesis]''' | ||
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 8.3 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 8.3 |
Revision as of 09:46, 16 February 2010
- Description: riboflavin kinase / FAD synthase
Gene name | ribC |
Synonyms | |
Essential | no |
Product | riboflavin kinase / FAD synthase |
Function | FAD biosynthesis |
Metabolic function and regulation of this protein in SubtiPathways: Riboflavin and FAD synthesis | |
MW, pI | 35 kDa, 8.3 |
Gene length, protein length | 948 bp, 316 aa |
Immediate neighbours | truB, rpsO |
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: BSU16670
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 + 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:
- Interactions:
- Localization:
Database entries
- UniProt: P54575
- KEGG entry: [2]
Additional information
Expression and regulation
- Operon:
- 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
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)