Difference between revisions of "HemH"
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] | ||
− | * ''' | + | * '''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 This image was kindly provided by SubtiList
|
Contents
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
- UniProt: P32396
- 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)