HEMH_SCHPO
ID HEMH_SCHPO Reviewed; 423 AA.
AC O59786;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 139.
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=hem15; ORFNames=SPCC320.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP GENE MODEL REVISION.
RX PubMed=24929437; DOI=10.1038/nsmb.2843;
RA Duncan C.D., Mata J.;
RT "The translational landscape of fission-yeast meiosis and sporulation.";
RL Nat. Struct. Mol. Biol. 21:641-647(2014).
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 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}. Note=Bound to the mitochondrial inner
CC membrane in eukaryotic cells with its active site on the matrix side of
CC the membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18311.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAA18311.1; ALT_SEQ; Genomic_DNA.
DR PIR; T41302; T41302.
DR RefSeq; NP_587720.1; NM_001022715.2.
DR AlphaFoldDB; O59786; -.
DR SMR; O59786; -.
DR BioGRID; 275770; 1.
DR STRING; 4896.SPCC320.09.1; -.
DR PaxDb; O59786; -.
DR PRIDE; O59786; -.
DR EnsemblFungi; SPCC320.09.1; SPCC320.09.1:pep; SPCC320.09.
DR GeneID; 2539199; -.
DR KEGG; spo:SPCC320.09; -.
DR PomBase; SPCC320.09; hem15.
DR VEuPathDB; FungiDB:SPCC320.09; -.
DR eggNOG; KOG1321; Eukaryota.
DR HOGENOM; CLU_018884_1_0_1; -.
DR InParanoid; O59786; -.
DR Reactome; R-SPO-189451; Heme biosynthesis.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:O59786; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
DR GO; GO:0004325; F:ferrochelatase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; ISO:PomBase.
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; Cytoplasm; Heme biosynthesis; Iron; Iron-sulfur; Lyase; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Nucleus;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..423
FT /note="Ferrochelatase, mitochondrial"
FT /id="PRO_0000008878"
FT ACT_SITE 385
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 47235 MW; F307E5B5262F6403 CRC64;
MIRFCPSCFA LKRTAPVLNH TSRLGNYFNN TFSKFSVNRM SVSSYSSDAS STVMDESPPN
GVTKSVSGKG PTAVVMMNMG GPSNLDEVGP FLERLFTDGD IIPLGYFQNS LGKFIAKRRT
PKVQNHYSDI GGGSPILHWT RIQGSEMCKI LDKKCPESAP HLPFVAFRYA PPLTEDMLDE
LKKANVSRAV AFSQYPQWSC ATSGASLNEL RRKLIEKGME KDFEWSIVDR WPLQQGLINA
FAENIEETLK TYPEDVRDDV VIVFSAHSLP MSQVAKGDPY VYEIAATSQA VMKRLNYKNK
FVNAWQSKVG PLPWMSPATD FVIEQLGNRG QKNMILVPIA FTSDHIETLK ELEDYIEDAK
QKGITGVKRV SSINGSMTAI QGMADLVAEH LKAKVPYSRQ FTQRCPGCTS ESCAERINFF
QDF
