Difference between revisions of "AraD"
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* '''Operon:''' ''[[araA]]-[[araB]]-[[araD]]-[[araL]]-[[araM]]-[[araN]]-[[araP]]-[[araQ]]-[[abfA]]'' {{PubMed|9084180}} | * '''Operon:''' ''[[araA]]-[[araB]]-[[araD]]-[[araL]]-[[araM]]-[[araN]]-[[araP]]-[[araQ]]-[[abfA]]'' {{PubMed|9084180}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=araD_2944983_2945672_-1 araD] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' [[SigA]] {{PubMed|9084180}} | ||
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 14:53, 16 April 2012
- Description: L-ribulose-phosphate 4-epimerase
Gene name | araD |
Synonyms | |
Essential | no |
Product | L-ribulose-phosphate 4-epimerase |
Function | arabinose utilization |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 25 kDa, 5.243 |
Gene length, protein length | 687 bp, 229 aa |
Immediate neighbours | araL, araB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
utilization of specific carbon sources
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28780
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-ribulose 5-phosphate = D-xylulose 5-phosphate (according to Swiss-Prot)
- Protein family: AraD/fucA subfamily (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: P94525
- KEGG entry: [3]
- E.C. number: 5.1.3.4
Additional information
Expression and regulation
- 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
José Manuel Inácio, Carla Costa, Isabel de Sá-Nogueira
Distinct molecular mechanisms involved in carbon catabolite repression of the arabinose regulon in Bacillus subtilis.
Microbiology (Reading): 2003, 149(Pt 9);2345-2355
[PubMed:12949161]
[WorldCat.org]
[DOI]
(P p)
L J Mota, P Tavares, I Sá-Nogueira
Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis.
Mol Microbiol: 1999, 33(3);476-89
[PubMed:10417639]
[WorldCat.org]
[DOI]
(P p)
Isabel Sa-Nogueira, Teresa V Nogueira, Snia Soares, Hermnia de Lencastre
The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression.
Microbiology (Reading): 1997, 143 ( Pt 3);957-969
[PubMed:9084180]
[WorldCat.org]
[DOI]
(P p)
I Sá-Nogueira, H de Lencastre
Cloning and characterization of araA, araB, and araD, the structural genes for L-arabinose utilization in Bacillus subtilis.
J Bacteriol: 1989, 171(7);4088-91
[PubMed:2500424]
[WorldCat.org]
[DOI]
(P p)