ID   CPFC_LACLA              Reviewed;         314 AA.
AC   Q9CFB4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
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}; Synonyms=hemH;
GN   OrderedLocusNames=LL1567; ORFNames=L0194;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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, ECO:0000305}.
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DR   EMBL; AE005176; AAK05665.1; -; Genomic_DNA.
DR   PIR; G86820; G86820.
DR   RefSeq; NP_267723.1; NC_002662.1.
DR   RefSeq; WP_003130709.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFB4; -.
DR   SMR; Q9CFB4; -.
DR   STRING; 272623.L0194; -.
DR   PaxDb; Q9CFB4; -.
DR   EnsemblBacteria; AAK05665; AAK05665; L0194.
DR   KEGG; lla:L0194; -.
DR   PATRIC; fig|272623.7.peg.1685; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_0_0_9; -.
DR   OMA; FSYHGVP; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000002196; Chromosome.
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; IPR033644; Ferrochelatase_C.
DR   InterPro; IPR033659; Ferrochelatase_N.
DR   PANTHER; PTHR11108; PTHR11108; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   TIGRFAMs; TIGR00109; hemH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..314
FT                   /note="Coproporphyrin III ferrochelatase"
FT                   /id="PRO_0000175152"
FT   BINDING         186
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         268
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   314 AA;  36436 MW;  00B03F49869B5E1F CRC64;
     MDKKKGILLV ALGTPRSCEA DDVRDYLKEF LGDPLVIQKP RWLWLPILNG IILKVRPQKS
     AEMYKKIWTD EGSPLMIYTV AQAKQLQDMR EDFDVRFAMT YGEPRIDKVI AEMKESGVEE
     ITVLPLYPQY SLTTVEPVIQ QVKKIDDKIK VIRDFHKVES YSDLLAESIR EKWQANDYDK
     LVLSYHGIPL SYVTKKKDAY EEQCKETTRL VVSKLGLREE EYEHTYQSKF GPEKWLEPAT
     IDRVAELPKE NAKKVLICSP AFVADCLETL FELEIENKEV FVENGGETFD FVHPFNDSLD
     FTRVLSEVVD QNRL