HEMH_YEAST
ID HEMH_YEAST Reviewed; 393 AA.
AC P16622; D6W2N2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 192.
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; OrderedLocusNames=YOR176W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2185242; DOI=10.1016/s0021-9258(19)39111-2;
RA Labbe-Bois R.;
RT "The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption,
RT and expression of its structural gene HEM15.";
RL J. Biol. Chem. 265:7278-7283(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2235498; DOI=10.1093/nar/18.20.6130;
RA Gokhman I., Zamir A.;
RT "The nucleotide sequence of the ferrochelatase and tRNA(val) gene region
RT from Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 18:6130-6130(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 32-51.
RX PubMed=3042776; DOI=10.1016/s0021-9258(18)37837-2;
RA Camadro J.-M., Labbe P.;
RT "Purification and properties of ferrochelatase from the yeast Saccharomyces
RT cerevisiae. Evidence for a precursor form of the protein.";
RL J. Biol. Chem. 263:11675-11682(1988).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
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 -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Matrix side. Note=It is bound to the mitochondrial inner
CC membrane in eukaryotic cells with its active site on the matrix side of
CC the membrane.
CC -!- PTM: The leader peptide may be processed in two proteolytic steps,
CC first between Ser-23 and Phe-24, second and by a different protease, to
CC yield the mature protein.
CC -!- MISCELLANEOUS: Ferrochelatase interacts with protoprophyrinogen
CC oxidase, and associates with complex 1 of the respiratory chain.
CC -!- MISCELLANEOUS: Acidic phospholipids or fatty acids are important for
CC the ferrochelatase activity.
CC -!- MISCELLANEOUS: Present with 22700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}.
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DR EMBL; J05395; AAA34667.1; -; Genomic_DNA.
DR EMBL; X54514; CAA38371.1; -; Genomic_DNA.
DR EMBL; Z75084; CAA99385.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10948.1; -; Genomic_DNA.
DR PIR; A35190; IBBYFC.
DR RefSeq; NP_014819.3; NM_001183595.3.
DR PDB; 1L8X; X-ray; 2.70 A; A/B=32-393.
DR PDB; 1LBQ; X-ray; 2.40 A; A/B=32-393.
DR PDB; 7L78; X-ray; 2.40 A; A/B=36-391.
DR PDBsum; 1L8X; -.
DR PDBsum; 1LBQ; -.
DR PDBsum; 7L78; -.
DR AlphaFoldDB; P16622; -.
DR SMR; P16622; -.
DR BioGRID; 34570; 40.
DR DIP; DIP-4133N; -.
DR IntAct; P16622; 7.
DR STRING; 4932.YOR176W; -.
DR iPTMnet; P16622; -.
DR MaxQB; P16622; -.
DR PaxDb; P16622; -.
DR PRIDE; P16622; -.
DR EnsemblFungi; YOR176W_mRNA; YOR176W; YOR176W.
DR GeneID; 854347; -.
DR KEGG; sce:YOR176W; -.
DR SGD; S000005702; HEM15.
DR VEuPathDB; FungiDB:YOR176W; -.
DR eggNOG; KOG1321; Eukaryota.
DR GeneTree; ENSGT00390000016258; -.
DR HOGENOM; CLU_018884_1_0_1; -.
DR InParanoid; P16622; -.
DR OMA; LGDPYHC; -.
DR BioCyc; YEAST:YOR176W-MON; -.
DR BRENDA; 4.99.1.1; 984.
DR Reactome; R-SCE-189451; Heme biosynthesis.
DR SABIO-RK; P16622; -.
DR UniPathway; UPA00252; UER00325.
DR EvolutionaryTrace; P16622; -.
DR PRO; PR:P16622; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P16622; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004325; F:ferrochelatase activity; IDA:SGD.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:SGD.
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 3D-structure; Direct protein sequencing; Heme biosynthesis; Iron; Lyase;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3042776"
FT CHAIN 32..393
FT /note="Ferrochelatase, mitochondrial"
FT /id="PRO_0000008879"
FT ACT_SITE 351
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 76..97
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 104..122
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 129..140
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:1LBQ"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1LBQ"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 203..218
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1LBQ"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 248..262
FT /evidence="ECO:0007829|PDB:1LBQ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:7L78"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1LBQ"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:1LBQ"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1LBQ"
SQ SEQUENCE 393 AA; 44596 MW; F04E7C7AAD36C24F CRC64;
MLSRTIRTQG SFLRRSQLTI TRSFSVTFNM QNAQKRSPTG IVLMNMGGPS KVEETYDFLY
QLFADNDLIP ISAKYQKTIA KYIAKFRTPK IEKQYREIGG GSPIRKWSEY QATEVCKILD
KTCPETAPHK PYVAFRYAKP LTAETYKQML KDGVKKAVAF SQYPHFSYST TGSSINELWR
QIKALDSERS ISWSVIDRWP TNEGLIKAFS ENITKKLQEF PQPVRDKVVL LFSAHSLPMD
VVNTGDAYPA EVAATVYNIM QKLKFKNPYR LVWQSQVGPK PWLGAQTAEI AEFLGPKVDG
LMFIPIAFTS DHIETLHEID LGVIGESEYK DKFKRCESLN GNQTFIEGMA DLVKSHLQSN
QLYSNQLPLD FALGKSNDPV KDLSLVFGNH EST
