YumC

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

electron transport/ other, essential genes

The gene

Basic information

• Locus tag: BSU32110

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Domains:

• Modification: active site Cys85 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus speciesPubMed

• Cofactors: FAD PubMed

• Effectors of protein activity:

• Interactions:
  • dimeric protein PubMed

• Localization:

Database entries

• Structure: 3LZW PubMed

• UniProt: O05268

• KEGG entry: [2]

• E.C. number: 1.18.1.2

Expression and regulation

• Operon:

• Expression browser: yumC PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)