Difference between revisions of "YumC"

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(Extended information on the protein)
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* '''Domains:'''  
 
* '''Domains:'''  
  
* '''Modification:'''
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* '''Modification:''' active site Cys85 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species[http://www.ncbi.nlm.nih.gov/pubmed/22938038 PubMed]
*** active site Cys85 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species[http://www.ncbi.nlm.nih.gov/pubmed/22938038 PubMed]
 
  
 
* '''Cofactor(s):''' FAD, NADPH {{PubMed|20878669}}
 
* '''Cofactor(s):''' FAD, NADPH {{PubMed|20878669}}

Revision as of 08:23, 6 September 2012

  • Description: ferredoxin-NAD(P)+ oxidoreductase

Gene name yumC
Synonyms
Essential yes PubMed
Product ferredoxin-NAD(P)+ oxidoreductase
Function redox reactions that involve ferredoxin
Gene expression levels in SubtiExpress: yumC
MW, pI 36 kDa, 5.573
Gene length, protein length 996 bp, 332 aa
Immediate neighbours yumB, yuzG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YumC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YumC expression.png
























Categories containing this gene/protein

electron transport/ other, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU32110

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 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH (according to Swiss-Prot)
  • Paralogous protein(s): YcgT

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: active site Cys85 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus speciesPubMed
  • Cofactor(s): FAD, NADPH PubMed
  • Effectors of protein activity:
  • Interactions: dimeric protein PubMed
  • Localization:

Database entries

  • KEGG entry: [2]
  • E.C. number:

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

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

Hirofumi Komori, Daisuke Seo, Takeshi Sakurai, Yoshiki Higuchi
Crystal structure analysis of Bacillus subtilis ferredoxin-NADP(+) oxidoreductase and the structural basis for its substrate selectivity.
Protein Sci: 2010, 19(12);2279-90
[PubMed:20878669] [WorldCat.org] [DOI] (I p)

Hirofumi Komori, Daisuke Seo, Takeshi Sakurai, Yoshiki Higuchi
Crystallization and preliminary X-ray studies of ferredoxin-NADP+ oxidoreductase encoded by Bacillus subtilis yumC.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 3);301-3
[PubMed:20208166] [WorldCat.org] [DOI] (I p)

Daisuke Seo, Seisuke Okabe, Mitsuhiro Yanase, Kunishige Kataoka, Takeshi Sakurai
Studies of interaction of homo-dimeric ferredoxin-NAD(P)+ oxidoreductases of Bacillus subtilis and Rhodopseudomonas palustris, that are closely related to thioredoxin reductases in amino acid sequence, with ferredoxins and pyridine nucleotide coenzymes.
Biochim Biophys Acta: 2009, 1794(4);594-601
[PubMed:19162251] [WorldCat.org] [DOI] (P p)

Daisuke Seo, Kei Kamino, Kazuhito Inoue, Hidehiro Sakurai
Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC.
Arch Microbiol: 2004, 182(1);80-9
[PubMed:15252706] [WorldCat.org] [DOI] (P p)