{PDOC00462}
{PS00534; FERROCHELATASE}
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* Ferrochelatase signature *
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Ferrochelatase (EC 4.99.1.1) (protoheme ferro-lyase) [1,2] catalyzes the  last
step in  heme  biosynthesis: the chelation of a ferrous ion to proto-porphyrin
IX, to form protoheme.

In eukaryotes,  ferrochelatase  is  a mitochondrial protein bound to the inner
membrane, whose active site faces the mitochondrial matrix. The mature form of
eukaryotic ferrochelatase  is  composed of about 360 amino acids. In bacteria,
ferrochelatase (gene hemH) [3] is a protein of from 310 to 380 amino acids.

The human autosomal  dominant  disease  protoporphyria  is  due to the reduced
activity of ferrochelatase.

The signature pattern for this enzyme is  based  on a conserved  region  which
contains a histidine residue which could be involved in binding iron.

-Consensus pattern: [LIVMF]-[LIVMFC]-x-[ST]-x-H-[GS]-[LIVM]-P-x(4,5)-
                    [DENQKRLHAFSTI]-x-[GN]-[DPC]-x(1,4)-[YA]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2004 / Pattern and text revised.

[ 1] Labbe-Bois R.
     J. Biol. Chem. 265:7278-7283(1990).
[ 2] Brenner D.A., Frasier F.
     "Cloning of murine ferrochelatase."
     Proc. Natl. Acad. Sci. U.S.A. 88:849-853(1991).
     PubMed=1704134
[ 3] Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.
     "Isolation and characterization of visible light-sensitive mutants of
     Escherichia coli K12."
     J. Mol. Biol. 219:393-398(1991).
     PubMed=2051480

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