ID   CPFC_STRPJ              Reviewed;         364 AA.
AC   B8ZPG2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Coproporphyrin III ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE            EC=4.99.1.9 {ECO:0000255|HAMAP-Rule:MF_00323};
GN   Name=cpfC {ECO:0000255|HAMAP-Rule:MF_00323}; OrderedLocusNames=SPN23F09340;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/jb.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA   Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA   Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-resistant
RT   pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(2009).
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the insertion of ferrous iron into coproporphyrin III to form
CC       Fe-coproporphyrin III. {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+);
CC         Xref=Rhea:RHEA:49572, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:68438, ChEBI:CHEBI:131725; EC=4.99.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00323};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00323};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00323}.
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DR   EMBL; FM211187; CAR68759.1; -; Genomic_DNA.
DR   RefSeq; WP_000709247.1; NC_011900.1.
DR   AlphaFoldDB; B8ZPG2; -.
DR   SMR; B8ZPG2; -.
DR   KEGG; sne:SPN23F09340; -.
DR   HOGENOM; CLU_018884_2_1_9; -.
DR   OMA; LGDPYHC; -.
DR   UniPathway; UPA00252; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
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   Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..364
FT                   /note="Coproporphyrin III ferrochelatase"
FT                   /id="PRO_1000189992"
FT   BINDING         29
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         118
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         169
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         250
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   364 AA;  42425 MW;  6A42C5C36EBD23D8 CRC64;
     MKKAILMMTF GSPEEITFEG VADFFTNIRR GVRPQDHEIQ TLYDNYVRIG GTPLQKITRQ
     EVALVEARLG NEYSVYFANK FSSPFIPDVI GQMEADGIEQ CICLILEPHY SFYSVMGYEK
     FLESKQIQFL VIKDWYQEEA LLNYWADEIA KILKEEVKQD SFKVIFSAHS VPIFALDFGD
     PYIDQIFENS KLVAEKLGLS SEQYTNTWQS ESDIGIPWIK PDVLEYLREQ TEHPDHYIFV
     PISFISEHIE VLFDNDVECY DLCQEFGVNY HRPPMPNTDS RLIDALVNTV RVNENQEFKE
     FLPEEETFDE LVPSDETKNI LAESEDLQMP EFVKKLIEKK GRENVKMPYL IKKMLEKAGK
     LPKE