Difference between revisions of "MhqA"
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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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| − | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mhqA_1353080_1354030_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:mhqA_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mhqA_1353080_1354030_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:mhqA_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU12870]] |
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU12870&redirect=T BSU12870] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mhqA.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mhqA.html] | ||
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* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
| − | * '''Protein family:''' extradiol ring-cleavage dioxygenase family (according to | + | * '''Protein family:''' extradiol ring-cleavage dioxygenase family (according to UniProt) |
* '''Paralogous protein(s):''' [[MhqE]], [[MhqO]] | * '''Paralogous protein(s):''' [[MhqE]], [[MhqO]] | ||
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU12870&redirect=T BSU12870] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3OAJ 3OAJ] ([[MhqO]], 34% identical residues) | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3OAJ 3OAJ] ([[MhqO]], 34% identical residues) | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 183 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = | ||
Latest revision as of 08:58, 25 June 2019
- 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 |
| Gene expression levels in SubtiExpress: mhqA | |
| MW, pI | 35 kDa, 5.404 |
| Gene length, protein length | 948 bp, 316 aa |
| Immediate neighbours | steT, ykcB |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU12870
Phenotypes of a mutant
Database entries
- BsubCyc: BSU12870
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: extradiol ring-cleavage dioxygenase family (according to UniProt)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU12870
- UniProt: O34689
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: mhqA PubMed
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 183 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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)
