Difference between revisions of "Ndh"
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* '''Interactions:''' | * '''Interactions:''' | ||
+ | ** [[Mdh]]-[[Ndh]] {{PubMed|20933603}} | ||
* '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | * '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
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=References= | =References= | ||
− | <pubmed>17015645,,11948165,18763711, </pubmed> | + | <pubmed>17015645,20933603,11948165,18763711, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:15, 13 October 2010
- Description: NADH dehydrogenase (Menaquinone 7 & no proton)
Gene name | ndh |
Synonyms | yjlD |
Essential | no |
Product | NADH dehydrogenase (Menaquinone 7 & no proton) |
Function | respiration |
MW, pI | 41 kDa, 6.289 |
Gene length, protein length | 1176 bp, 392 aa |
Immediate neighbours | yjlC, uxaC |
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: BSU12290
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
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:
- Cofactor(s):
- Effectors of protein activity:
- Localization: membrane associated PubMed
Database entries
- Structure:
- UniProt: P80861
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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, 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)