Ndh

• Description: NADH dehydrogenase (Menaquinone 7 & no proton)
  
  

Gene name	ndh
Synonyms	yjlD
Essential	no
Product	NADH dehydrogenase (Menaquinone 7 & no proton)
Function	respiration
Gene expression levels in SubtiExpress: ndh
Interactions involving this protein in SubtInteract: Ndh
MW, pI	41 kDa, 6.289
Gene length, protein length	1176 bp, 392 aa
Immediate neighbours	yjlC, uxaC
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

respiration, membrane proteins, most abundant proteins

This gene is a member of the following regulons

Rex regulon, stringent response

The gene

Basic information

• Locus tag: BSU12290

Database entries

• BsubCyc: BSU12290

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: NADH dehydrogenase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • Mdh-Ndh PubMed

• Localization: membrane associated PubMed

Database entries

• BsubCyc: BSU12290

• Structure:

• UniProt: P80861

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: yjlC-ndh PubMed

• Expression browser: ndh PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed
  • induced under anaerobic conditions (Rex) PubMed

• Regulatory mechanism:
  • Rex: transcription repression PubMed
• Additional information:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Frederik M Meyer, Jan Gerwig, Elke Hammer, Christina Herzberg, Fabian M Commichau, Uwe Völker, Jörg Stülke
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon.
Metab Eng: 2011, 13(1);18-27
[PubMed:20933603] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Smita Gyan, Yoshihiko Shiohira, Ichiro Sato, Michio Takeuchi, Tsutomu Sato
Regulatory loop between redox sensing of the NADH/NAD(+) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis.
J Bacteriol: 2006, 188(20);7062-71
[PubMed:17015645] [WorldCat.org] [DOI] (P 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)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)