YumC

From SubtiWiki
Revision as of 18:41, 18 February 2014 by Jstuelk (talk | contribs) (Basic information/ Evolution)
Jump to: navigation, search
  • 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)
  • Protein family: ferredoxin--NADP reductase type 2 family (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)