TuaD

• Description: UDP glucose 6-dehydrogenase
  
  

Gene name	tuaD
Synonyms	yvhD
Essential	no
Product	UDP glucose 6-dehydrogenase
Function	biosynthesis of teichuronic acid
MW, pI	49 kDa, 6.107
Gene length, protein length	1383 bp, 461 aa
Immediate neighbours	tuaE, tuaC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components

This gene is a member of the following regulons

PhoP regulon

The gene

Basic information

• Locus tag: BSU35580

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: UDP-glucose + 2 NAD⁺ + H₂O = UDP-glucuronate + 2 NADH (according to Swiss-Prot)

• Protein family: UDP-glucose/GDP-mannose dehydrogenase family (according to Swiss-Prot)

• Paralogous protein(s): YtcA, Ugd

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on a Tyr residue by PtkA PubMed, dephosphorylated by PtpZ PubMed

• Cofactor(s):

• Effectors of protein activity: PtkA-dependent phosphorylation stimulates TuaD activity PubMed

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: O32271

• KEGG entry: [3]

• E.C. number: 1.1.1.22

Expression and regulation

• Operon: tuaA-tuaB-tuaC-tuaD-tuaE-tuaF-tuaG-tuaH PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed under conditions of phosphate limitation (PhoP) PubMed

• Regulatory mechanism:
  • PhoP: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ivan Mijakovic, Lucia Musumeci, Lutz Tautz, Dina Petranovic, Robert A Edwards, Peter Ruhdal Jensen, Tomas Mustelin, Josef Deutscher, Nunzio Bottini
In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.
J Bacteriol: 2005, 187(10);3384-90
[PubMed:15866923] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Sandrine Poncet, Grégory Boël, Alain Mazé, Sylvie Gillet, Emmanuel Jamet, Paulette Decottignies, Christophe Grangeasse, Patricia Doublet, Pierre Le Maréchal, Josef Deutscher
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
EMBO J: 2003, 22(18);4709-18
[PubMed:12970183] [WorldCat.org] [DOI] (P p)

H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081] [WorldCat.org] [DOI] (P p)

Maryam Lahooti, Colin R Harwood
Transcriptional analysis of the Bacillus subtilis teichuronic acid operon.
Microbiology (Reading): 1999, 145 ( Pt 12);3409-3417
[PubMed:10627039] [WorldCat.org] [DOI] (P p)

Marco Pagni, Vladimir Lazarevic, Blazenka Soldo, Dimitri Karamata
Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in teichuronic acid synthesis.
Microbiology (Reading): 1999, 145 ( Pt 5);1049-1053
[PubMed:10376820] [WorldCat.org] [DOI] (P p)

B Soldo, V Lazarevic, M Pagni, D Karamata
Teichuronic acid operon of Bacillus subtilis 168.
Mol Microbiol: 1999, 31(3);795-805
[PubMed:10048024] [WorldCat.org] [DOI] (P p)

Wei Liu, F Marion Hulett
Comparison of PhoP binding to the tuaA promoter with PhoP binding to other Pho-regulon promoters establishes a Bacillus subtilis Pho core binding site.
Microbiology (Reading): 1998, 144 ( Pt 5);1443-1450
[PubMed:9611818] [WorldCat.org] [DOI] (P p)