Difference between revisions of "YumC"

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(Database entries)
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''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]
 
* '''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]
  
* '''Cofactor(s):''' FAD, NADPH {{PubMed|20878669}}
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* '''[[Cofactors]]:''' FAD {{PubMed|20878669}}
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' dimeric protein {{PubMed|20878669}}
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* '''[[SubtInteract|Interactions]]:'''
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** dimeric protein {{PubMed|20878669}}
  
* '''Localization:'''
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* '''[[Localization]]:'''
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yumC_3301586_3302584_1 yumC] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yumC_3301586_3302584_1 yumC] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
  
<pubmed>22938038, 20208166, 20878669, 19162251, 15252706 </pubmed>
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<pubmed>22938038, 20208166, 20878669, 19162251, 15252706 24529496 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:40, 18 February 2014

  • 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
Sequences Protein DNA DNA_with_flanks
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:
  • Modification: active site Cys85 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus speciesPubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • 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

Daisuke Seo, Tomoya Asano, Hirofumi Komori, Takeshi Sakurai
Role of the C-terminal extension stacked on the re-face of the isoalloxazine ring moiety of the flavin adenine dinucleotide prosthetic group in ferredoxin-NADP(+) oxidoreductase from Bacillus subtilis.
Plant Physiol Biochem: 2014, 81;143-8
[PubMed:24529496] [WorldCat.org] [DOI] (I p)

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)