Difference between revisions of "HmoB"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
| − | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' binds hemin ''in vitro'' with ~1:1 stoichiometry and degrade hemin in the presence of an electron donor {{PubMed|21873409}} |
* '''Protein family:''' | * '''Protein family:''' | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
| − | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' ''[[ | + | * '''Operon:''' ''[[hmoB]]'' {{PubMed|8335642}} |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| + | ** constitutively expressed {{PubMed|21873409}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
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=References= | =References= | ||
| − | <pubmed> 8335642 </pubmed> | + | <pubmed> 8335642 21873409</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 07:12, 30 August 2011
- Description: heme monooxygenase
| Gene name | hmoB |
| Synonyms | yixC, yhgC |
| Essential | no |
| Product | heme monooxygenase |
| Function | degradation of heme |
| MW, pI | 18 kDa, 5.216 |
| Gene length, protein length | 498 bp, 166 aa |
| Immediate neighbours | yhgB, pbpF |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- 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
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)
