HmoB

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  • 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
Metabolic function and regulation of this protein in SubtiPathways:
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
YhgC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HmoB expression.png

Contents















Categories containing this gene/protein

acquisition of iron

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

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 727 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1160 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 6764 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5260 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5763 PubMed

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] (I p)

Ahmed Gaballa, John D Helmann
Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.
Microbiology (Reading, Engl.): 2011, 157(Pt 11);3221-31
[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] (P p)

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