Difference between revisions of "Dra"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1MZH 1MZH] (from ''Aquifex aeolicus'', 42% identity, 62% similarity) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39121 P39121] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P39121 P39121] |
Revision as of 11:49, 19 February 2010
- Description: deoxyribose-phosphate aldolase
Gene name | dra |
Synonyms | |
Essential | no |
Product | deoxyribose-phosphate aldolase |
Function | utilization of nucleotides as carbon source |
Metabolic function and regulation of this protein in SubtiPathways: Nucleoside catabolism, Nucleotides (regulation) | |
MW, pI | 22 kDa, 4.926 |
Gene length, protein length | 633 bp, 211 aa |
Immediate neighbours | nupC, deoR |
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: BSU39420
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde (according to Swiss-Prot)
- Protein family: DeoC type 1 subfamily (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
- Structure: 1MZH (from Aquifex aeolicus, 42% identity, 62% similarity)
- UniProt: P39121
- KEGG entry: [3]
- E.C. number: 4.1.2.4
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
Xianmin Zeng, Anne Galinier, Hans H Saxild
Catabolite repression of dra-nupC-pdp operon expression in Bacillus subtilis.
Microbiology (Reading): 2000, 146 ( Pt 11);2901-2908
[PubMed:11065368]
[WorldCat.org]
[DOI]
(P p)
Y Miwa, A Nakata, A Ogiwara, M Yamamoto, Y Fujita
Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis.
Nucleic Acids Res: 2000, 28(5);1206-10
[PubMed:10666464]
[WorldCat.org]
[DOI]
(I p)
X Zeng, H H Saxild
Identification and characterization of a DeoR-specific operator sequence essential for induction of dra-nupC-pdp operon expression in Bacillus subtilis.
J Bacteriol: 1999, 181(6);1719-27
[PubMed:10074062]
[WorldCat.org]
[DOI]
(P p)
H H Saxild, L N Andersen, K Hammer
Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein.
J Bacteriol: 1996, 178(2);424-34
[PubMed:8550462]
[WorldCat.org]
[DOI]
(P p)