DhbA

• Description: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
  
  

Gene name	dhbA
Synonyms	entA
Essential	no
Product	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
Function	biosynthesis of the siderophore bacillibactin
MW, pI	27 kDa, 5.311
Gene length, protein length	783 bp, 261 aa
Immediate neighbours	dhbC, besA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

acquisition of iron, iron metabolism

This gene is a member of the following regulons

Fur regulon

The gene

Basic information

• Locus tag: BSU32000

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2,3-dihydro-2,3-dihydroxybenzoate + NAD⁺ = 2,3-dihydroxybenzoate + NADH (according to Swiss-Prot)

• Protein family: short-chain dehydrogenases/reductases (SDR) 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: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P39071

• KEGG entry: [3]

• E.C. number: 1.3.1.28

Expression and regulation

• Operon: dhbA-dhbC-dhbE-dhbB-dhbF PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by iron starvation (Fur) PubMed

• Regulatory mechanism:
  • Fur: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229] [WorldCat.org] [DOI] (P p)

Tamara Hoffmann, Alexandra Schütz, Margot Brosius, Andrea Völker, Uwe Völker, Erhard Bremer
High-salinity-induced iron limitation in Bacillus subtilis.
J Bacteriol: 2002, 184(3);718-27
[PubMed:11790741] [WorldCat.org] [DOI] (P p)

J J May, T M Wendrich, M A Marahiel
The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin.
J Biol Chem: 2001, 276(10);7209-17
[PubMed:11112781] [WorldCat.org] [DOI] (P p)

N Bsat, J D Helmann
Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo.
J Bacteriol: 1999, 181(14);4299-307
[PubMed:10400588] [WorldCat.org] [DOI] (P p)

B M Rowland, T H Grossman, M S Osburne, H W Taber
Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes.
Gene: 1996, 178(1-2);119-23
[PubMed:8921902] [WorldCat.org] [DOI] (P p)

B M Rowland, H W Taber
Duplicate isochorismate synthase genes of Bacillus subtilis: regulation and involvement in the biosyntheses of menaquinone and 2,3-dihydroxybenzoate.
J Bacteriol: 1996, 178(3);854-61
[PubMed:8550523] [WorldCat.org] [DOI] (P p)

R Adams, W Schumann
Cloning and mapping of the Bacillus subtilis locus homologous to Escherichia coli ent genes.
Gene: 1993, 133(1);119-21
[PubMed:8224884] [WorldCat.org] [DOI] (P p)