CPFC_CORDI
ID CPFC_CORDI Reviewed; 369 AA.
AC Q6NH66;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=DIP1280;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248357; CAE49807.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6NH66; -.
DR SMR; Q6NH66; -.
DR STRING; 257309.DIP1280; -.
DR EnsemblBacteria; CAE49807; CAE49807; DIP1280.
DR KEGG; cdi:DIP1280; -.
DR HOGENOM; CLU_018884_2_0_11; -.
DR OMA; WLEPDIC; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002198; 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; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..369
FT /note="Coproporphyrin III ferrochelatase"
FT /id="PRO_0000175132"
FT BINDING 61
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 130
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 197
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 286
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 369 AA; 41046 MW; 1202EC393E0DFB9D CRC64;
MLPLPTWTLS DVDAILVLSF GGPEGQQDVI PFLENVTRGR GIPRERLEEV AVHYRHFGGI
SPLNALNREI IGNIIEVLSS RGLEIPVYFG NRNWHPFVND TAEKMVRDGV RNVAVFATSA
WGGYSGCRQY DEDIVRMNHH LEEKELPTLN CLKLRQFFDH PLFIEEMSSV VFQAARELGI
SALDELQLHQ KVVFTAHSIP EVANENSGRK EDGPLYSRQV YEAASLVAKH LGISQERYDV
VWQSASGNGQ IPWLEPDILD YAKCQHDEGV SELVVAPIGF ISDHMEVVWD LDHELQDLAS
DLGMSISRAA TVGHTDSFAT MIVELVEESL GVKPHQNLGT VPSKGCSFNG EPCEVNCCKP
VQRPHSAKA