HemH

From SubtiWiki
Revision as of 12:54, 16 May 2013 by 134.76.70.252 (talk)
Jump to: navigation, search
  • 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
Sequences Protein DNA DNA_with_flanks
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

Yaxue Wang, Yong Shen
Is it possible for Fe2+ to approach protoporphyrin IX from the side of Tyr-13 in Bacillus subtilis ferrochelatase? An answer from QM/MM study.
J Mol Model: 2013, 19(2);963-71
[PubMed:23097001] [WorldCat.org] [DOI] (I p)

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)

Mattias D Hansson, Mats Lindstam, Mats Hansson
Crosstalk between metal ions in Bacillus subtilis ferrochelatase.
J Biol Inorg Chem: 2006, 11(3);325-33
[PubMed:16453119] [WorldCat.org] [DOI] (P 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)