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
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
























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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • 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

Additional references: PubMed

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)

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)