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