Difference between revisions of "HemH"

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* '''Description:''' ferrochelatase <br/><br/>
 
 
 
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Revision as of 13:21, 9 August 2012

  • Description: ferrochelatase

Gene name hemH
Synonyms hemF
Essential no
Product ferrochelatase
Function heme biosynthesis
Gene expression levels in SubtiExpress: hemH
MW, pI 35 kDa, 4.617
Gene length, protein length 930 bp, 310 aa
Immediate neighbours hemE, hemY
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
HemH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HemH expression.png
























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU10130

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: insertion of Fe(2+) into protoporphyrin IX
  • Protein family: ferrochelatase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 2HK6 (complex with iron), 1AK1
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • 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

Mattias D Hansson, Tobias Karlberg, Christopher A G Söderberg, Sreekanth Rajan, Martin J Warren, Salam Al-Karadaghi, Stephen E J Rigby, Mats Hansson
Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase.
J Biol Inorg Chem: 2011, 16(2);235-42
[PubMed:21052751] [WorldCat.org] [DOI] (I p)

S Al-Karadaghi, M Hansson, S Nikonov, B Jönsson, L Hederstedt
Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis.
Structure: 1997, 5(11);1501-10
[PubMed:9384565] [WorldCat.org] [DOI] (P p)

M Hansson, L Hederstedt
Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis.
Eur J Biochem: 1994, 220(1);201-8
[PubMed:8119288] [WorldCat.org] [DOI] (P p)

M Hansson, L Hederstedt
Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes.
J Bacteriol: 1992, 174(24);8081-93
[PubMed:1459957] [WorldCat.org] [DOI] (P p)