HEMH_DICDI
ID HEMH_DICDI Reviewed; 423 AA.
AC Q54IA8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ferrochelatase, mitochondrial;
DE EC=4.99.1.1;
DE AltName: Full=Heme synthase;
DE AltName: Full=Protoheme ferro-lyase;
DE Flags: Precursor;
GN Name=hemH; ORFNames=DDB_G0288891;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
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; AAFI02000126; EAL62969.1; -; Genomic_DNA.
DR RefSeq; XP_636471.1; XM_631379.1.
DR AlphaFoldDB; Q54IA8; -.
DR SMR; Q54IA8; -.
DR STRING; 44689.DDB0231413; -.
DR PaxDb; Q54IA8; -.
DR EnsemblProtists; EAL62969; EAL62969; DDB_G0288891.
DR GeneID; 8626854; -.
DR KEGG; ddi:DDB_G0288891; -.
DR dictyBase; DDB_G0288891; hemH.
DR eggNOG; KOG1321; Eukaryota.
DR HOGENOM; CLU_018884_1_0_1; -.
DR InParanoid; Q54IA8; -.
DR OMA; LGDPYHC; -.
DR PhylomeDB; Q54IA8; -.
DR Reactome; R-DDI-189451; Heme biosynthesis.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:Q54IA8; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004325; F:ferrochelatase activity; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; ISS:dictyBase.
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 3: Inferred from homology;
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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..423
FT /note="Ferrochelatase, mitochondrial"
FT /id="PRO_0000327542"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 380
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 404
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"
SQ SEQUENCE 423 AA; 47990 MW; 16089D79F5CD2FAF CRC64;
MISRKIISTI NSKTFYNKSL SYCTVNNNKN TTININNNNE KPKIKTGILM LNLGGPSKLE
EVEPFLTRLF TDKEIFKLPF QKYTGTLIAK RRSNAVMKLY EAIGGGSPIR KWTEKQGELL
SSMMDKISPE TAPHKHYIGF RYSDPLIADT LDQMENDNVE RVVAFSQYPQ YSCTTTGSSL
NNLWKTLEEK QMQSKFKWSV IDRWQDHKGF IDATIHKIKK AYNQFNSKLR ELDIDDVDAN
NNNNNNKPVL VFSAHSLPMS TVEKGDPYPQ EVAETVCRVM DGLGIRDEET GKPLEYILAW
QSKVGPLPWL SPKTSFVIEQ LAKKGRNAIV IPIAFTSDHI ETLSEIDIEL QHLAKKCGMK
LLVRSESLND DPLIISAMAD LVNTHLKSNK TIHSNQYHLK CPGCKDDSTF CRTISNPIQA
LKL
