NrdF

• Description: ribonucleoside-diphosphate reductase (major subunit)
  
  

Gene name	nrdF
Synonyms
Essential	yes PubMed
Product	ribonucleoside-diphosphate reductase (major subunit)
Function	synthesis of deoxyribonucleoside triphosphates
Gene expression levels in SubtiExpress: nrdF
Interactions involving this protein in SubtInteract: NrdF
Metabolic function and regulation of this protein in SubtiPathways: nrdF
MW, pI	38 kDa, 4.66
Gene length, protein length	987 bp, 329 aa
Immediate neighbours	nrdE, ymaB
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

biosynthesis/ acquisition of nucleotides, essential genes

This gene is a member of the following regulons

ResD regulon

The gene

Basic information

• Locus tag: BSU17390

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU17390

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H₂O = ribonucleoside diphosphate + thioredoxin (according to Swiss-Prot)

• Protein family: ribonucleoside diphosphate reductase small chain family (according to Swiss-Prot)

• Paralogous protein(s): YosP

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:
  • Mn(2+) PubMed
  • dimanganic-tyrosyl radical (Mn^III₂-Y•) cofactor PubMed

• Effectors of protein activity:

• Interactions:
  • NrdE-NrdF PubMed
  • NrdI-NrdF PubMed

• Localization:

Database entries

• BsubCyc: BSU17390

• Structure: 4DR0 PubMed

• UniProt: P50621

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: nrdI-nrdE-nrdF-ymaB PubMed

• Expression browser: nrdF PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed under anaerobic conditions (ResD) PubMed

• Regulatory mechanism:
  • ResD: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Elisabeth Härtig, Braunschweig, Germany Homepage

References

Reviews

John Herrick, Bianca Sclavi
Ribonucleotide reductase and the regulation of DNA replication: an old story and an ancient heritage.
Mol Microbiol: 2007, 63(1);22-34
[PubMed:17229208] [WorldCat.org] [DOI] (P p)

Original Publications

Mackenzie J Parker, Xuling Zhu, JoAnne Stubbe
Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.
Biochemistry: 2014, 53(4);766-76
[PubMed:24401092] [WorldCat.org] [DOI] (I p)

Joseph A Cotruvo, Troy A Stich, R David Britt, JoAnne Stubbe
Mechanism of assembly of the dimanganese-tyrosyl radical cofactor of class Ib ribonucleotide reductase: enzymatic generation of superoxide is required for tyrosine oxidation via a Mn(III)Mn(IV) intermediate.
J Am Chem Soc: 2013, 135(10);4027-39
[PubMed:23402532] [WorldCat.org] [DOI] (I p)

Amie K Boal, Joseph A Cotruvo, Joanne Stubbe, Amy C Rosenzweig
The dimanganese(II) site of Bacillus subtilis class Ib ribonucleotide reductase.
Biochemistry: 2012, 51(18);3861-71
[PubMed:22443445] [WorldCat.org] [DOI] (I p)

Yan Zhang, Joanne Stubbe
Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.
Biochemistry: 2011, 50(25);5615-23
[PubMed:21561096] [WorldCat.org] [DOI] (I p)

Elisabeth Härtig, Anja Hartmann, Manuela Schätzle, Alessandra M Albertini, Dieter Jahn
The Bacillus subtilis nrdEF genes, encoding a class Ib ribonucleotide reductase, are essential for aerobic and anaerobic growth.
Appl Environ Microbiol: 2006, 72(8);5260-5
[PubMed:16885274] [WorldCat.org] [DOI] (P p)

C Scotti, A Valbuzzi, M Perego, A Galizzi, A M Albertini
The Bacillus subtilis genes for ribonucleotide reductase are similar to the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae.
Microbiology (Reading): 1996, 142 ( Pt 11);2995-3004
[PubMed:8969495] [WorldCat.org] [DOI] (P p)