ID   CPFC_STAEQ              Reviewed;         307 AA.
AC   Q5HNA5;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=SERP1367;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54744.1; -; Genomic_DNA.
DR   RefSeq; WP_001829846.1; NC_002976.3.
DR   AlphaFoldDB; Q5HNA5; -.
DR   SMR; Q5HNA5; -.
DR   STRING; 176279.SERP1367; -.
DR   EnsemblBacteria; AAW54744; AAW54744; SERP1367.
DR   GeneID; 50018413; -.
DR   KEGG; ser:SERP1367; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_2_1_9; -.
DR   OMA; LGDPYHC; -.
DR   OrthoDB; 780534at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000000531; 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; 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; Reference proteome.
FT   CHAIN           1..307
FT                   /note="Coproporphyrin III ferrochelatase"
FT                   /id="PRO_0000175208"
FT   BINDING         12
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         29
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         45..46
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         53
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         124
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         181
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         263
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   307 AA;  35429 MW;  0A8B9B6DB549B06B CRC64;
     MTKTIGLLVM AYGTPYKESD IEPYYTDIRR GKKPTEEELQ DLKDRYEFIG GLSPLAGTTD
     RQAEALLEAL NKEQDDVNFK LYLGLKHISP YIEEAVEQMH NDGIKEAVTV VLAPHYSSFS
     VGSYDQRAQE KADEYGIQLT HIKHYYQQPK FIKYWTEKIN ETLEQIPNQE HDETVLVVSA
     HSLPKGLIER NNDPYPHELH ETAEILKQES NIIHVAEGWQ SEGNTGTPWL GPDVQDLTRD
     LYKEHQFKHF IYTPVGFVCE HLEVLYDNDY ECKVVCDDIG VNYYRPEMPN THPLFIGAIV
     DEIQSHI