Difference between revisions of "HemH"

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Line 78: Line 78:
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2HK6 2HK6] (complex with iron),  [http://www.rcsb.org/pdb/explore.do?structureId=1AK1 1AK1]
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2HK6 2HK6] (complex with iron),  [http://www.rcsb.org/pdb/explore.do?structureId=1AK1 1AK1]
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P32396 P32396]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P32396 P32396]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU10130]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU10130]

Revision as of 11:47, 20 July 2009

  • Description: Ferrochelatase

Gene name hemH
Synonyms hemF
Essential no
Product Ferrochelatase
Function heme biosynthesis
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



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: Protoheme + 2 H+ = protoporphyrin + Fe2+ (according to Swiss-Prot)
  • 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:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • 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

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)