HEMH_PANTR
ID HEMH_PANTR Reviewed; 423 AA.
AC Q3YA36;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16385445; DOI=10.1086/498620;
RA Gouya L., Martin-Schmitt C., Robreau A.-M., Austerlitz F., Da Silva V.,
RA Brun P., Simonin S., Lyoumi S., Grandchamp B., Beaumont C., Puy H.,
RA Deybach J.-C.;
RT "Contribution of a common single-nucleotide polymorphism to the genetic
RT predisposition for erythropoietic protoporphyria.";
RL Am. J. Hum. Genet. 78:2-14(2006).
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; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P22830};
CC -!- ACTIVITY REGULATION: Inhibited by nitric oxide (NO). The 2Fe-2S cluster
CC could act as a NO sensor (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity). Interaction with PGRMC1; the
CC interaction results in decreased FECH activity (By similarity).
CC Interacts with ABCB10 and SLC25A37; this interaction forms an
CC oligomeric complex (By similarity). Forms a complex with ABCB7 and
CC ABCB10, where a dimeric FECH bridges ABCB7 and ABCB10 homodimers; this
CC complex may be required for cellular iron homeostasis, mitochondrial
CC function and heme biosynthesis. Interacts with ABCB7 and ABCB10 (By
CC similarity). {ECO:0000250|UniProtKB:P22315,
CC 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; DQ149645; AAZ78230.1; -; mRNA.
DR RefSeq; NP_001033101.1; NM_001038012.1.
DR AlphaFoldDB; Q3YA36; -.
DR SMR; Q3YA36; -.
DR STRING; 9598.ENSPTRP00000054886; -.
DR PaxDb; Q3YA36; -.
DR GeneID; 455437; -.
DR KEGG; ptr:455437; -.
DR CTD; 2235; -.
DR eggNOG; KOG1321; Eukaryota.
DR InParanoid; Q3YA36; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW 2Fe-2S; Acetylation; Heme biosynthesis; Iron; Iron-sulfur; Lyase; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 55..423
FT /note="Ferrochelatase, mitochondrial"
FT /id="PRO_0000232439"
FT ACT_SITE 230
FT /evidence="ECO:0000250"
FT ACT_SITE 383
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22315"
FT MOD_RES 138
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22315"
FT MOD_RES 415
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22315"
FT MOD_RES 415
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22315"
SQ SEQUENCE 423 AA; 47964 MW; 2ABA551586F7E7CC CRC64;
MRSLGANMAA ALRAAGVLLR DPLVSSSWRV YQPWRWKSVA AAAAATTETA QHAQGAKPQV
QPQKRKPKTG ILMLNMGGPE TLGDVHDFLL RLFLDRDLMT LPIQNKLAPF IAKRRTPKIQ
EQYRRIGGGS PIKIWTSKQG EGMVKLLDEL SPNTAPHKYY IGFRYVHPLT EEAIEEMERD
GLERAIAFTQ YPQYSCSTTG SSLNAIYRYY NQVGRKPTMK WSTIDRWPTH HLLIQCFADH
ILKELDHFPL EKRSEVVILF SAHSLPMSVV NRGDPYPQEV SATVQKVMER LEYCNPYRLV
WQSKVGPMPW LGPQTDESIK GLCERGRKNI LLVPIAFTSD HIETLYELDI EYSQVLAKEC
GVENIRRAES LNGNPLFSKA LADLVHSHIQ SNELCSKQLT LSCPLCVNPV CRETKSFFTS
QQL
