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CPFC_PROFF
ID   CPFC_PROFF              Reviewed;         352 AA.
AC   P72183;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 92.
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;
OS   Propionibacterium freudenreichii subsp. freudenreichii.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=66712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC
RC   10470 / NRRL B-3523;
RX   PubMed=9163953; DOI=10.1007/s002530050945;
RA   Hashimoto Y., Yamashita Y., Murooka Y.;
RT   "The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes
RT   enzymes and a regulator involved in the biosynthetic pathway from glutamate
RT   to protoheme.";
RL   Appl. Microbiol. Biotechnol. 47:385-392(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-352.
RA   Roessner C.A.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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; D85417; BAA21910.1; -; Genomic_DNA.
DR   EMBL; U51164; AAB07862.1; -; Genomic_DNA.
DR   RefSeq; WP_044636334.1; NZ_CP010341.1.
DR   AlphaFoldDB; P72183; -.
DR   SMR; P72183; -.
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..352
FT                   /note="Coproporphyrin III ferrochelatase"
FT                   /id="PRO_0000175179"
FT   BINDING         52
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         121
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         178
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         267
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   352 AA;  37456 MW;  8FC67D73A801ACBA CRC64;
     MTSFDALLVA GFGGPESMAE VPDFLQRVSG GHIPPDRLAE VEHHYARFGG VSPVNAQHRA
     LAAALGEALV ARGIDVPIAN ANRHSMPYMD QALADLQSRG IRRVLTLVPT PYASYSGCRA
     YREELLAGTR IDDEGRPALQ VVKLDPYADL PALVTAQVQL LRAALADHPD AHLVFTTHSI
     PTAMAETSGP HGNAYIPQHL ALIDAVMAEL AALGLRPSWE LAYQSRSGSP RTPWLEPDIN
     DVITRLAGEG VRDVICSPIG FLTDHMEVVW DLDTEAAATA AEHSMAFTRV ATVGTLPVFI
     EGLADLIVAA LSTKPGTGPD APAARHWCTP DCCPNARIAG RPTIPGFAAG PR
 
 
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