Difference between revisions of "DhbA"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU32000 dhbA]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU32000 dhbA]
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=DhbA DhbA]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 5.311   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 5.311   

Revision as of 11:51, 8 April 2014

  • 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
Gene expression levels in SubtiExpress: dhbA
Metabolic function and regulation of this protein in SubtiPathways:
DhbA
MW, pI 27 kDa, 5.311
Gene length, protein length 783 bp, 261 aa
Immediate neighbours dhbC, besA
Sequences Protein DNA DNA_with_flanks
Genetic context
DhbA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DhbA expression.png















Categories containing this gene/protein

acquisition of iron, iron metabolism

This gene is a member of the following regulons

AbrB regulon, Fur regulon

The gene

Basic information

  • Locus tag: BSU32000

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)

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)