Difference between revisions of "NadD"
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| + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=nadD_2643765_2644334_-1 nadD] {{PubMed|22383849}} | ||
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=Biological materials = | =Biological materials = | ||
Revision as of 11:43, 16 April 2012
- Description: nicotinamide-nucleotide adenylyltransferase
| Gene name | nadD |
| Synonyms | yqeJ |
| Essential | yes PubMed |
| Product | nicotinamide-nucleotide adenylyltransferase |
| Function | NAD biosynthesis |
| MW, pI | 22 kDa, 5.123 |
| Gene length, protein length | 567 bp, 189 aa |
| Immediate neighbours | yqeK, yqeI |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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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: BSU25640
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 + nicotinate ribonucleotide = diphosphate + deamido-NAD+ (according to Swiss-Prot)
- Protein family: nadD 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
- Structure: 1KAQ
- UniProt: P54455
- KEGG entry: [2]
- E.C. number: 2.7.7.18
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
Andrea M Olland, Kathryn W Underwood, Robert M Czerwinski, Mei-Chu Lo, Ann Aulabaugh, Joel Bard, Mark L Stahl, William S Somers, Francis X Sullivan, Rajiv Chopra
Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase.
J Biol Chem: 2002, 277(5);3698-707
[PubMed:11704676]
[WorldCat.org]
[DOI]
(P p)
