Difference between revisions of "HmoB"
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yhgC_1083229_1083729_-1 hmoB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yhgC_1083229_1083729_-1 hmoB] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 17:13, 4 March 2014
- Description: heme monooxygenase
| Gene name | hmoB |
| Synonyms | yixC, yhgC |
| Essential | no |
| Product | heme monooxygenase |
| Function | degradation of heme, acquisition of iron |
| Gene expression levels in SubtiExpress: hmoB | |
| MW, pI | 18 kDa, 5.216 |
| Gene length, protein length | 498 bp, 166 aa |
| Immediate neighbours | yhgB, pbpF |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU10100
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: binds hemin in vitro with ~1:1 stoichiometry and degrade hemin in the presence of an electron donor PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- UniProt: P38049
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- constitutively expressed PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Seonghun Park, Dajeong Kim, Inae Jang, Han Bin Oh, Jungwoo Choe
Structural and biochemical study of Bacillus subtilis HmoB in complex with heme.
Biochem Biophys Res Commun: 2014, 446(1);286-91
[PubMed:24582752]
[WorldCat.org]
[DOI]
(I p)
Seonghun Park, Sarah Choi, Jungwoo Choe
Bacillus subtilis HmoB is a heme oxygenase with a novel structure.
BMB Rep: 2012, 45(4);239-41
[PubMed:22531134]
[WorldCat.org]
[DOI]
(I p)
Ahmed Gaballa, John D Helmann
Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.
Microbiology (Reading): 2011, 157(Pt 11);3221-3231
[PubMed:21873409]
[WorldCat.org]
[DOI]
(I p)
D L Popham, P Setlow
Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class A high-molecular-weight penicillin-binding protein.
J Bacteriol: 1993, 175(15);4870-6
[PubMed:8335642]
[WorldCat.org]
[DOI]
(P p)
