The domain within your query sequence starts at position 67 and ends at position 388; the E-value for the Ferrochelatase domain shown below is 5.9e-115.

KTGILMLNMGGPETLGEVQDFLQRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIG
GGSPIKMWTSKQGEGMVKLLDELSPATAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIA
FTQYPQYSCSTTGSSLNAIYRYYNEVGQKPTMKWSTIDRWPTHPLLIQCFADHILKELNH
FPEEKRSEVVILFSAHSLPMSVVNRGDPYPQEVGATVHKVMEKLGYPNPYRLVWQSKVGP
VPWLGPQTDEAIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAQKCGAENIRR
AESLNGNPLFSKALADLVHSHI

Ferrochelatase

 Ferrochelatase
PFAM accession number:PF00762
Interpro abstract (IPR001015):

Synonym(s): Protohaem ferro-lyase, Iron chelatase, etc.

Ferrochelatase is the terminal enzyme of the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into the protoporphyrin IX ring yielding protoheme. This enzyme is ubiquitous in nature and widely distributed in bacteria and eukaryotes. Recently, some archaeal members have been identified. The oligomeric state of these enzymes varies depending on the presence of a dimerization motif at the C terminus [ (PUBMED:12196143) (PUBMED:11215517) (PUBMED:10582332) (PUBMED:8122254) (PUBMED:6390167) (PUBMED:7592569) (PUBMED:11175906) (PUBMED:12427010) (PUBMED:10704318) (PUBMED:12761666) (PUBMED:2185242) (PUBMED:1704134) ]. In eukaryotic cells, it binds to the mitochondrial inner membrane with its active site on the matrix side of the membrane.

The X-ray structure of Bacillus subtilis and human ferrochelatase have been solved [ (PUBMED:9384565) (PUBMED:11175906) ]. The human enzyme exists as a homodimer. Each subunit contains one [2Fe-2S] cluster. The monomer is folded into two similar domains, each with a four-stranded parallel beta-sheet flanked by an alpha-helix in a beta-alpha-beta motif that is reminiscent of the fold found in the periplasmic binding proteins. The topological similarity between the domains suggests that they have arisen from a gene duplication event. However, significant differences exist between the two domains, including an N-terminal section (residues 80-130) that forms part of the active site pocket, and a C-terminal extension (residues 390-423) that is involved in coordination of the [2Fe-2S] cluster and in stabilisation of the homodimer.

Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals. Porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme. It is likely that the structure of the cleft region will have different conformations upon substrate binding and release [ (PUBMED:9384565) ].

GO process:heme biosynthetic process (GO:0006783)
GO function:ferrochelatase activity (GO:0004325)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ferrochelatase