HEMH_CHICK
ID HEMH_CHICK Reviewed; 402 AA.
AC O42479;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=White leghorn;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U68033; AAB66503.1; -; mRNA.
DR RefSeq; NP_989527.1; NM_204196.1.
DR AlphaFoldDB; O42479; -.
DR SMR; O42479; -.
DR STRING; 9031.ENSGALP00000004832; -.
DR PaxDb; O42479; -.
DR GeneID; 374020; -.
DR KEGG; gga:374020; -.
DR CTD; 2235; -.
DR VEuPathDB; HostDB:geneid_374020; -.
DR eggNOG; KOG1321; Eukaryota.
DR InParanoid; O42479; -.
DR OrthoDB; 1003638at2759; -.
DR PhylomeDB; O42479; -.
DR BRENDA; 4.99.1.1; 1306.
DR Reactome; R-GGA-421984; Heme synthesis.
DR SABIO-RK; O42479; -.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:O42479; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..402
FT /note="Ferrochelatase, mitochondrial"
FT /id="PRO_0000008875"
FT ACT_SITE 209
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 382
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 45430 MW; 3C30BA86CE1C3993 CRC64;
MAAAGRAARP LVAGGRQLRV PLRWRGQVAA AAPSTKPQAE PETRKPKTGI LMLNMGGPER
LDDVHDFLLR LFLDRDLMTL PAQNKLAPFI AKRRTPRIQE QYSRIGGGSP IKKWTAVQGE
GMVKLLDSMS PQTAPHKYYI GFRYVHPLTE EAIEEMEDDG IERAIAFTQY PQYSCSTTGS
SLNAIYRYYN KKGKKPKMKW SIIDRWPTHP LLIQCFADHI QKELDLFPPD KRKDVVILFS
AHSLPMSVVN RGDPYPQEVG ATVQRVMEKL NHSNPYRLVW QSKVGPMPWL VPQTDETIKG
LCQRGKKNML LVPIAFTSDH IETLYELDIE YAQVLANECG VENIRRAESL NGNPLFSKAL
ADLVCSHIQS NEICSKQLTL CCPLCVNPVC RETKAFFTNQ QL
