HemH

• Description: ferrochelatase
  
  

Gene name	hemH
Synonyms	hemF
Essential	no
Product	ferrochelatase
Function	heme biosynthesis
Gene expression levels in SubtiExpress: hemH
Metabolic function and regulation of this protein in SubtiPathways: 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of cofactors

The gene

Basic information

• Locus tag: BSU10130

Database entries

• BsubCyc: BSU10130

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU10130

• Structure: 2HK6 (complex with iron), 1AK1

• UniProt: P32396

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hemE-hemH-hemY PubMed

• Expression browser: hemH PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 83 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1426 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1547 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1289 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1239 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)