Difference between revisions of "DapB"
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− | * '''Operon:''' | + | * '''Operon:''' ''[[ypjD]]-[[dapB]]-[[mgsA]]-[[bshB2]]-[[bshA]]-[[cca]]-[[birA]]'' {{PubMed|20308541}} |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
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=References= | =References= | ||
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+ | <pubmed> 20308541 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:12, 7 April 2010
- Description: dihydrodipicolinate reductase (NADPH)
Gene name | dapB |
Synonyms | |
Essential | yes PubMed |
Product | dihydrodipicolinate reductase (NADPH) |
Function | biosynthesis of lysine and peptidoglycan |
Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr | |
MW, pI | 29 kDa, 5.057 |
Gene length, protein length | 801 bp, 267 aa |
Immediate neighbours | mgsA, ypjD |
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: BSU22490
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: 2,3,4,5-tetrahydrodipicolinate + NAD(P)+ = 2,3-dihydrodipicolinate + NAD(P)H (according to Swiss-Prot)
- Protein family: glucose-6-phosphate dehydrogenase 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: P42976
- KEGG entry: [2]
- E.C. number: 1.3.1.26
Additional information
Expression and regulation
- 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
Operon and expression
Ahmed Gaballa, Gerald L Newton, Haike Antelmann, Derek Parsonage, Heather Upton, Mamta Rawat, Al Claiborne, Robert C Fahey, John D Helmann
Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli.
Proc Natl Acad Sci U S A: 2010, 107(14);6482-6
[PubMed:20308541]
[WorldCat.org]
[DOI]
(I p)