MhqA

• Description: hydroquinone-specific dioxygenase, confers resistence to methyl-hydroxyquinone
  
  

Gene name	mhqA
Synonyms	ykcA
Essential	no
Product	hydroquinone-specific dioxygenase
Function	resistence to methyl-hydroxyquinone
MW, pI	35 kDa, 5.404
Gene length, protein length	948 bp, 316 aa
Immediate neighbours	steT, ykcB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

resistance against oxidative and electrophile stress

This gene is a member of the following regulons

MhqR regulon

The gene

Basic information

• Locus tag: BSU12870

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: extradiol ring-cleavage dioxygenase family (according to Swiss-Prot)

• Paralogous protein(s): MhqE, MhqO

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: 3OAJ (MhqO, 34% identical residues)

• UniProt: O34689

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: mhqA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by catechol and 2-methylhydroquinone (MhqR) PubMed

• Regulatory mechanism:
  • MhqR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Stefanie Töwe, Montira Leelakriangsak, Kazuo Kobayashi, Nguyen Van Duy, Michael Hecker, Peter Zuber, Haike Antelmann
The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis.
Mol Microbiol: 2007, 66(1);40-54
[PubMed:17725564] [WorldCat.org] [DOI] (P p)

Van Duy Nguyen, Carmen Wolf, Ulrike Mäder, Michael Lalk, Peter Langer, Ulrike Lindequist, Michael Hecker, Haike Antelmann
Transcriptome and proteome analyses in response to 2-methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems involved in the catabolism of aromatic compounds in Bacillus subtilis.
Proteomics: 2007, 7(9);1391-408
[PubMed:17407181] [WorldCat.org] [DOI] (P p)