RibD

• Description: 5-amino-6-(5-phosphoribosylamino)uracil reductase
  
  

Gene name	ribD
Synonyms	ribG
Essential	no
Product	5-amino-6-(5-phosphoribosylamino)uracil reductase
Function	riboflavin biosynthesis
Gene expression levels in SubtiExpress: ribD
Metabolic function and regulation of this protein in SubtiPathways: Riboflavin / FAD
MW, pI	39 kDa, 6.079
Gene length, protein length	1083 bp, 361 aa
Immediate neighbours	ribE, ypuD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

FMN-box

The gene

Basic information

• Locus tag: BSU23280

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H₂O = 5-amino-6-(5-phosphoribosylamino)uracil + NH₃ (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 3EX8 PubMed

• UniProt: P17618

• KEGG entry: [3]

• E.C. number: 3.5.4.26, 1.1.1.193

Expression and regulation

• Operon: ribD-ribE-ribA-ribH-ribT PubMed

• Expression browser: ribD PubMed

• Sigma factor: SigA PubMed

• Regulation: expressed in the absence of FMN (FMN-box) PubMed

• Regulatory mechanism: FMN-box: riboswitch, mediates termination/ antitermination control of the operon, in the absence of FMN: antitermination, in the presence of FMN: termination PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Sheng Chia Chen, Chieh Yi Shen, Te Ming Yen, Hui Chia Yu, Ting Hao Chang, Wen Lin Lai, Shwu Huey Liaw
Evolution of vitamin B2 biosynthesis: eubacterial RibG and fungal Rib2 deaminases.
Acta Crystallogr D Biol Crystallogr: 2013, 69(Pt 2);227-36
[PubMed:23385458] [WorldCat.org] [DOI] (I p)

S A Skliarova, R A Kreneva, D A Perumov, A S Mironov
[The characterization of internal promoters in the Bacillus subtilis riboflavin biosynthesis operon].
Genetika: 2012, 48(10);1133-41
[PubMed:23270261] [WorldCat.org] (P p)

Sheng-Chia Chen, Yu-Hsin Lin, Hui-Chia Yu, Shwu-Huey Liaw
Complex structure of Bacillus subtilis RibG: the reduction mechanism during riboflavin biosynthesis.
J Biol Chem: 2009, 284(3);1725-31
[PubMed:18986985] [WorldCat.org] [DOI] (P p)

J Kenneth Wickiser, Wade C Winkler, Ronald R Breaker, Donald M Crothers
The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch.
Mol Cell: 2005, 18(1);49-60
[PubMed:15808508] [WorldCat.org] [DOI] (P p)

Wade C Winkler, Smadar Cohen-Chalamish, Ronald R Breaker
An mRNA structure that controls gene expression by binding FMN.
Proc Natl Acad Sci U S A: 2002, 99(25);15908-13
[PubMed:12456892] [WorldCat.org] [DOI] (P p)

V N Mironov, A S Kraev, M L Chikindas, B K Chernov, A I Stepanov, K G Skryabin
Functional organization of the riboflavin biosynthesis operon from Bacillus subtilis SHgw.
Mol Gen Genet: 1994, 242(2);201-8
[PubMed:8159171] [WorldCat.org] [DOI] (P p)

V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830] [WorldCat.org] [DOI] (P p)