BdhA

• Description: acetoine/ butanediol dehydrogenase
  
  

Gene name	bdhA
Synonyms	ydjL
Essential	no
Product	acetoine/ butanediol dehydrogenase
Function	overflow metabolism, fermentation
Gene expression levels in SubtiExpress: bdhA
MW, pI	37 kDa, 4.805
Gene length, protein length	1038 bp, 346 aa
Immediate neighbours	iolT, ydjM
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

• Locus tag: BSU06240

Database entries

• BsubCyc: BSU06240

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: formation of butanediol from acetoin PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-13 PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU06240

• Structure:

• UniProt: O34788

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: bdhA (according to DBTBS)

• Expression browser: bdhA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:
  • AbrB: transcription repression PubMed

• Additional information:
  • The mRNA has a long (268 nt) untranslated leader region PubMed
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Xian Zhang, Teng Bao, Zhiming Rao, Taowei Yang, Zhenghong Xu, Shangtian Yang, Huazhong Li
Two-stage pH control strategy based on the pH preference of acetoin reductase regulates acetoin and 2,3-butanediol distribution in Bacillus subtilis.
PLoS One: 2014, 9(3);e91187
[PubMed:24608678] [WorldCat.org] [DOI] (I e)

Rafael R de Oliveira, Wayne L Nicholson
The LysR-type transcriptional regulator (LTTR) AlsR indirectly regulates expression of the Bacillus subtilis bdhA gene encoding 2,3-butanediol dehydrogenase.
Appl Microbiol Biotechnol: 2013, 97(16);7307-16
[PubMed:23576037] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Ranjita Biswas, Masaru Yamaoka, Hideki Nakayama, Takashi Kondo, Ken-ichi Yoshida, Virendra S Bisaria, Akihiko Kondo
Enhanced production of 2,3-butanediol by engineered Bacillus subtilis.
Appl Microbiol Biotechnol: 2012, 94(3);651-8
[PubMed:22361854] [WorldCat.org] [DOI] (I p)

Claudia Frädrich, Anika March, Kerstin Fiege, Anja Hartmann, Dieter Jahn, Elisabeth Härtig
The transcription factor AlsR binds and regulates the promoter of the alsSD operon responsible for acetoin formation in Bacillus subtilis.
J Bacteriol: 2012, 194(5);1100-12
[PubMed:22178965] [WorldCat.org] [DOI] (I p)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Wayne L Nicholson
The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-butanediol dehydrogenase.
Appl Environ Microbiol: 2008, 74(22);6832-8
[PubMed:18820069] [WorldCat.org] [DOI] (I p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)