ID   HEMH_XENLA              Reviewed;         411 AA.
AC   O57478;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Ferrochelatase, mitochondrial {ECO:0000250|UniProtKB:P22830};
DE            EC=4.99.1.1 {ECO:0000250|UniProtKB:P22830};
DE   AltName: Full=Heme synthase;
DE   AltName: Full=Protoheme ferro-lyase;
DE   Flags: Precursor;
GN   Name=fech {ECO:0000250|UniProtKB:P22830};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=9808757; DOI=10.1006/abbi.1998.0910;
RA   Day A.L., Parsons B.M., Dailey H.A.;
RT   "Cloning and characterization of Gallus and Xenopus ferrochelatases:
RT   presence of the [2Fe-2S] cluster in nonmammalian ferrochelatase.";
RL   Arch. Biochem. Biophys. 359:160-169(1998).
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC       {ECO:0000250|UniProtKB:P22830}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC         Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P22830};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P22830};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P22830}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P22315}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P22315}; Matrix side
CC       {ECO:0000250|UniProtKB:P22315}.
CC   -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}.
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DR   EMBL; AF036617; AAB94626.1; -; mRNA.
DR   AlphaFoldDB; O57478; -.
DR   SMR; O57478; -.
DR   BRENDA; 4.99.1.1; 6725.
DR   SABIO-RK; O57478; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004325; F:ferrochelatase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00419; Ferrochelatase_C; 1.
DR   CDD; cd03411; Ferrochelatase_N; 1.
DR   HAMAP; MF_00323; Ferrochelatase; 1.
DR   InterPro; IPR001015; Ferrochelatase.
DR   InterPro; IPR019772; Ferrochelatase_AS.
DR   InterPro; IPR033644; Ferrochelatase_C.
DR   InterPro; IPR033659; Ferrochelatase_N.
DR   PANTHER; PTHR11108; PTHR11108; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   TIGRFAMs; TIGR00109; hemH; 1.
DR   PROSITE; PS00534; FERROCHELATASE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Heme biosynthesis; Iron; Iron-sulfur; Lyase; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..411
FT                   /note="Ferrochelatase, mitochondrial"
FT                   /id="PRO_0000008876"
FT   REGION          34..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        217
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         390
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46039 MW;  010A1C422697A2B3 CRC64;
     MAAFRAAHRL LGHILRNESS AGLVTQRWSS SAAVASVPKS SDPKPHAQPD KRKPKTGILM
     LNMGGPETLD DVHGFLLRLF LDKDLMTLPA QSKLAPFIAK RRTPKIQEQY SKIGGGSPIK
     KWTEQQGEGM VKLLDELSPA TAPHKYYIGF RYVRPLTEAA IEEMERDGVE RAIAFTQYPQ
     YSCSTTGSSL NAIYRYYNAK GTQPKMKWSV IDRWPTHPLL IQCFADHIQK ELNMFPADKR
     GEVVILFSAH SLPMSVVNRG DPYPQEVGAT VQKVMERLGF SNPYRLVWQS KVGPMAWLGP
     QTDESIKGLC QRGKKNILLV PIAFTSDHIE TLYELDIEYA QVLAKECGVE NIRRSESLNG
     NPLFSKALAD LVLSHMKSSE ICSKQLSLRC PMCVNPVCGE AKSFFTKQQQ Q