FrlD

• Description: fructosamine kinase
  
  

Gene name	frlD
Synonyms	yurL
Essential	no
Product	fructosamine kinase
Function	metabolism of sugar amines
Gene expression levels in SubtiExpress: frlD
Metabolic function and regulation of this protein in SubtiPathways: frlD
MW, pI	30 kDa, 4.909
Gene length, protein length	852 bp, 284 aa
Immediate neighbours	frlR, frlM
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

utilization of specific carbon sources, utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

CodY regulon, FrlR regulon

The gene

Basic information

• Locus tag: BSU32570

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: carbohydrate kinase pfkB family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O32153

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • frlB-frlO-frlN-frlM-frlD PubMed

• Expression browser: frlD PubMed

• Sigma factor:

• Regulation:
  • frlB: repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • frlB: induced in the presence of fructosamine (FrlR) PubMed

• Regulatory mechanism:
  • CodY: transcription repression PubMed1, PubMed2
  • FrlR: transcription repression PubMed

• Additional information:
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
  • the frlB-frlO-frlN-frlM-frlD operon is not expressed in a cshA mutant PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Martin Lehnik-Habrink, Leonie Rempeters, Ákos T Kovács, Christoph Wrede, Claudia Baierlein, Heike Krebber, Oscar P Kuipers, Jörg Stülke
DEAD-Box RNA helicases in Bacillus subtilis have multiple functions and act independently from each other.
J Bacteriol: 2013, 195(3);534-44
[PubMed:23175651] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Veronika Maria Deppe, Stephanie Klatte, Johannes Bongaerts, Karl-Heinz Maurer, Timothy O'Connell, Friedhelm Meinhardt
Genetic control of amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR.
Appl Environ Microbiol: 2011, 77(9);2839-46
[PubMed:21398478] [WorldCat.org] [DOI] (I p)

Veronika Maria Deppe, Johannes Bongaerts, Timothy O'Connell, Karl-Heinz Maurer, Friedhelm Meinhardt
Enzymatic deglycation of Amadori products in bacteria: mechanisms, occurrence and physiological functions.
Appl Microbiol Biotechnol: 2011, 90(2);399-406
[PubMed:21347729] [WorldCat.org] [DOI] (I p)

Elsa Wiame, Pedro Lamosa, Helena Santos, Emile Van Schaftingen
Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine.
Biochem J: 2005, 392(Pt 2);263-9
[PubMed:16153181] [WorldCat.org] [DOI] (I p)

Elsa Wiame, Armelle Duquenne, Ghislain Delpierre, Emile Van Schaftingen
Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis.
FEBS Lett: 2004, 577(3);469-72
[PubMed:15556630] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)