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: ribD
MW, pI	39 kDa, 6.079
Gene length, protein length	1083 bp, 361 aa
Immediate neighbours	ribE, ypuD
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 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

Additional publications: PubMed

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)