CPFC1_BACC1
ID CPFC1_BACC1 Reviewed; 311 AA.
AC Q73C98;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Coproporphyrin III ferrochelatase 1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.9 {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=cpfC1 {ECO:0000255|HAMAP-Rule:MF_00323}; OrderedLocusNames=BCE_1168;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS40098.1; -; Genomic_DNA.
DR RefSeq; WP_000726783.1; NC_003909.8.
DR AlphaFoldDB; Q73C98; -.
DR SMR; Q73C98; -.
DR EnsemblBacteria; AAS40098; AAS40098; BCE_1168.
DR GeneID; 59157247; -.
DR KEGG; bca:BCE_1168; -.
DR HOGENOM; CLU_018884_2_1_9; -.
DR OMA; LGDPYHC; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002527; 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.
FT CHAIN 1..311
FT /note="Coproporphyrin III ferrochelatase 1"
FT /id="PRO_0000175104"
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 182
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 311 AA; 35339 MW; 25B6D263536C2844 CRC64;
MKKKIGLLVM AYGTPYKEED IERYYTHIRR GRKPSPEMLE DLTERYRAIG GISPLATITL
EQAKKLEKRL NEVQDEVEYH MYLGLKHIEP FIEDAVKDMH NDGIQDAIAL VLAPHYSTFS
VKSYVGRAQE EAEKLGNLTI HGIDSWYKEP KFIQYWVDAV KGIYNGMSDA EREKAVLIVS
AHSLPEKIIA MGDPYPEQLH ETADYIARGA EVANYAVGWQ SAGNTPDPWI GPDVQDLTRE
LNEKHGYTSF VYAPVGFVAE HLEVLYDNDF ECKVVTDEIG AKYYRPEMPN ASDAFIDCLT
DVVLKKKESV L
