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IPR001015

Description

IPR001015 is a Ferrochelatase.

<p>Synonym(s): Protohaem ferro-lyase, Iron chelatase, etc. <p>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 [[cite:PUB00012956], [cite:PUB00079463], [cite:PUB00079464], [cite:PUB00079466], [cite:PUB00079467], [cite:PUB00079465], [cite:PUB00006693], [cite:PUB00022076], [cite:PUB00021315], [cite:PUB00026989], [cite:PUB00002620], [cite:PUB00004754]]. In eukaryotic cells, it binds to the mitochondrial inner membrane with its active site on the matrix side of the membrane.</p> <p>The X-ray structure of<i>Bacillus subtilis</i>and human ferrochelatase have been solved [[cite:PUB00006691], [cite:PUB00006693]]. 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 β-sheet flanked by an α-helix in a β-α-β 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.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function Ferrochelatase activity Catalysis of the reaction: protoheme = Fe(2+) + protoporphyrin IX.
Biological process Heme biosynthetic process The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.

Associated Lotus transcripts 19

Transcript Name Description Predicted domains Domain count
PREDICTED: ferrochelatase-2, chloroplastic-like [Cicer arietinum] gi|502139638|ref|XP_004503842.1| 20
PREDICTED: ferrochelatase-2, chloroplastic-like [Glycine max] gi|356506948|ref|XP_003522235.1| 17
PREDICTED: ferrochelatase-2, chloroplastic-like [Cicer arietinum] gi|502156234|ref|XP_004510373.1| 13
Ferrochelatase [Medicago truncatula] gi|357520255|ref|XP_003630416.1| 19
PREDICTED: ferrochelatase-2, chloroplastic-like [Glycine max] gi|356506948|ref|XP_003522235.1| 17
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|O04921|HEMH2_ARATH Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|V7AZZ3|V7AZZ3_PHAVU Ferrochelatase; Found in the gene: LotjaGi1g1v0328100 18
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|Q0DIV0|HEMH2_ORYSJ Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|V7AZZ3|V7AZZ3_PHAVU Ferrochelatase; Found in the gene: LotjaGi1g1v0328100 11
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|O04921|HEMH2_ARATH Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|I1KBS4|I1KBS4_SOYBN Ferrochelatase; Found in the gene: LotjaGi1g1v0328100 17
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|O04921|HEMH2_ARATH Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|I1KBS4|I1KBS4_SOYBN Ferrochelatase; Found in the gene: LotjaGi1g1v0328100 17
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|O04921|HEMH2_ARATH Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|I1KBS4|I1KBS4_SOYBN Ferrochelatase; Found in the gene: LotjaGi1g1v0328100 17
Ferrochelatase; TAIR: AT5G26030.1 ferrochelatase 1; Swiss-Prot: sp|P42044|HEMH_CUCSA Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|I1JTV8|I1JTV8_SOYBN Ferrochelatase; Found in the gene: LotjaGi1g1v0366200 17
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|Q0DIV0|HEMH2_ORYSJ Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|G7LGG4|G7LGG4_MEDTR Ferrochelatase; Found in the gene: LotjaGi4g1v0415800 17
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|Q0DIV0|HEMH2_ORYSJ Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|A0A151SU66|A0A151SU66_CAJCA Ferrochelatase; Found in the gene: LotjaGi4g1v0415800 11
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|Q0DIV0|HEMH2_ORYSJ Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|A0A151SU66|A0A151SU66_CAJCA Ferrochelatase; Found in the gene: LotjaGi4g1v0415800 11
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|O04921|HEMH2_ARATH Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|K7KRA8|K7KRA8_SOYBN Ferrochelatase; Found in the gene: LotjaGi4g1v0415800 17
Ferrochelatase; TAIR: AT2G30390.1 ferrochelatase 2; Swiss-Prot: sp|Q0DIV0|HEMH2_ORYSJ Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|G7LGG4|G7LGG4_MEDTR Ferrochelatase; Found in the gene: LotjaGi4g1v0415800 17
Ferrochelatase; TAIR: AT5G26030.1 ferrochelatase 1; Swiss-Prot: sp|P42044|HEMH_CUCSA Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|A0A0B2RCX6|A0A0B2RCX6_GLYSO Ferrochelatase; Found in the gene: LotjaGi6g1v0043700 21
Ferrochelatase; TAIR: AT5G26030.1 ferrochelatase 1; Swiss-Prot: sp|P42044|HEMH_CUCSA Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|A0A0B2RCX6|A0A0B2RCX6_GLYSO Ferrochelatase; Found in the gene: LotjaGi6g1v0043700 17
Ferrochelatase; TAIR: AT5G26030.1 ferrochelatase 1; Swiss-Prot: sp|P42044|HEMH_CUCSA Ferrochelatase-2, chloroplastic; TrEMBL-Plants: tr|A0A0B2RCX6|A0A0B2RCX6_GLYSO Ferrochelatase; Found in the gene: LotjaGi6g1v0043700 17

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
cd03411 CDD 1 5.26