CPFC_TROW8
ID CPFC_TROW8 Reviewed; 391 AA.
AC Q83H94;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=TW747;
OS Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=218496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW08/27;
RX PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA Relman D.A.;
RT "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT Tropheryma whipplei.";
RL Lancet 361:637-644(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; BX251412; CAD67406.1; -; Genomic_DNA.
DR RefSeq; WP_011096684.1; NC_004551.1.
DR AlphaFoldDB; Q83H94; -.
DR SMR; Q83H94; -.
DR PRIDE; Q83H94; -.
DR GeneID; 67388528; -.
DR KEGG; tws:TW747; -.
DR HOGENOM; CLU_018884_2_0_11; -.
DR OMA; WLEPDIC; -.
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 PROSITE; PS00534; FERROCHELATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis.
FT CHAIN 1..391
FT /note="Coproporphyrin III ferrochelatase"
FT /id="PRO_0000175220"
FT BINDING 79
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 148
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 211
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 305
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 391 AA; 43521 MW; F4AEADA970393847 CRC64;
MIRRSAVSRV VAEGSAIASD SGFALGASQY DAVVLLSFGG PEGPEDVVPF LKKVTSGRGV
PDERLYEVAE HYNHFSGISP INDCNRRLRG ALEKELFSRG IRIPVLWANR NWQPQLEEVL
REAYDRGFRA FLTLFTSAYS CYSSCRQYRE DIAHAVERAG LSGRIIVDKL RQFFDHPGFV
LPFIEGIQDC LEQVKERGFK VSRTAILFST HSIPELDAAF SGPEDAHFGK YGAYVSQHKA
VVEVIMSRLR VTDPDLQNYQ LVYQSRSGDP STPWLEPDIN DAIRVLRGCE AVLIVPLGFI
SDHMEVLWDL DNESMQTARE CGLFAIRTPT PGTHPLYISG MVDLIVERLE GVPRSARPAM
TDLGPWFDVC QPGCCKNSRS GFKPAYGGVA P