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CPFC_MYCLE
ID   CPFC_MYCLE              Reviewed;         336 AA.
AC   Q9CBM2;
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, hemZ;
GN   OrderedLocusNames=ML1805;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(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; AL583923; CAC30758.1; -; Genomic_DNA.
DR   PIR; F87134; F87134.
DR   RefSeq; NP_302226.1; NC_002677.1.
DR   RefSeq; WP_010908547.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBM2; -.
DR   SMR; Q9CBM2; -.
DR   STRING; 272631.ML1805; -.
DR   EnsemblBacteria; CAC30758; CAC30758; CAC30758.
DR   KEGG; mle:ML1805; -.
DR   PATRIC; fig|272631.5.peg.3430; -.
DR   Leproma; ML1805; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_2_0_11; -.
DR   OMA; WLEPDIC; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000000806; 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..336
FT                   /note="Coproporphyrin III ferrochelatase"
FT                   /id="PRO_0000175165"
FT   BINDING         52
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         116
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         176
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         259
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   336 AA;  36314 MW;  D5F3E7D63F8C13FF CRC64;
     MLFDAALLLS FGGPDGPEQV RPFLENVTRG CNVPPERLDE VTKHYLHFGG VSPINGINLA
     LVNELQVELD LPVYFGNRNW EPYIEDSVVT MRDDGIRCAA VFITSAWSGY SSCTRYVEAI
     ARARRRAGTG APNLVKLRPY FDHPLFVEMF VDAITAAAAS LPAALRSEAR LVFTAHSVPV
     ATDRRCGPAL YSRQVGYAAR LVAAGAGYAD YDLTWQSRSG PPYVPWLAPD VGDQLMTLAS
     AGTKAVIVCP IGFVADHIEV VWDLDHELRS QADAAGVAFA RAATPNADRR FARLAASLID
     ELTHDRVPVR VNGSDPVPGC LASINGVPCD LPHCVA
 
 
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