HmoB

• Description: heme monooxygenase
  
  

Gene name	hmoB
Synonyms	yixC, yhgC
Essential	no
Product	heme monooxygenase
Function	degradation of heme, acquisition of iron
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
Expression at a glance   PubMed

Categories containing this gene/protein

acquisition of iron

The gene

Basic information

• Locus tag: BSU10100

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:

Database entries

• Structure: 3TVZ PubMed

• UniProt: P38049

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hmoB PubMed

• Expression browser: hmoB PubMed

• Sigma factor:

• Regulation:
  • constitutively expressed PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)