RibA

• Description: GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone 4-phosphate synthase
  
  

Gene name	ribA
Synonyms
Essential	no
Product	GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone 4-phosphate synthase
Function	riboflavin biosynthesis
MW, pI	43 kDa, 5.582
Gene length, protein length	1194 bp, 398 aa
Immediate neighbours	ribH, ribE
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU23260

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate (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: 2BZ0 (from E. coli, 54% identity, 69% similarity to the C-terminal domain) PubMed

• UniProt: P17620

• KEGG entry: [3]

• E.C. number: 3.5.4.25, 4.1.99.12

Expression and regulation

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

Martin Lehmann, Simone Degen, Hans-Peter Hohmann, Markus Wyss, Adelbert Bacher, Nicholas Schramek
Biosynthesis of riboflavin. Screening for an improved GTP cyclohydrolase II mutant.
FEBS J: 2009, 276(15);4119-29
[PubMed:19583770] [WorldCat.org] [DOI] (I p)

Jingshan Ren, Masayo Kotaka, Michael Lockyer, Heather K Lamb, Alastair R Hawkins, David K Stammers
GTP cyclohydrolase II structure and mechanism.
J Biol Chem: 2005, 280(44);36912-9
[PubMed:16115872] [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)

A Sorokin, E Zumstein, V Azevedo, S D Ehrlich, P Serror
The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data.
Mol Microbiol: 1993, 10(2);385-95
[PubMed:7934829] [WorldCat.org] [DOI] (P p)