CPFC_COREF
ID CPFC_COREF Reviewed; 377 AA.
AC Q8FTB1;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
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=CE1658;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC18468.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC18468.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006767659.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FTB1; -.
DR SMR; Q8FTB1; -.
DR STRING; 196164.23493498; -.
DR EnsemblBacteria; BAC18468; BAC18468; BAC18468.
DR KEGG; cef:CE1658; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_2_0_11; -.
DR OrthoDB; 780534at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001409; 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.
DR TIGRFAMs; TIGR00109; hemH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..377
FT /note="Coproporphyrin III ferrochelatase"
FT /id="PRO_0000175133"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 131
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 194
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 282
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 377 AA; 41872 MW; 5F9C9EDD3DB652CC CRC64;
MNARTPDTKS DSYDALLVLS FGGPEGPEEV RPFLENVTRG RGIPPERLDE VGAHYYHFGG
VSPLNRLNKE IIANVKAELA ARGYDIPVYF GNRNWKPFDN EAAEQMAADG IRNALVFATS
AWGGYSGCRQ YHEDIQGMRA HLEEIGAPEV TFTKLRQFYD HPRFVRTMAQ YVRESFDKLP
EDLRDEARLV FTAHSIPLNS KDADGNPIDG SIYSRQVEES SALIAREAGI DDFDVVWQSR
SGSPHVPWLE PDIVDHAVEL NENNGQKALV VCPVGFISDH MEVIWDLDSE LMDEATRRGM
VIERVATVGP SDEFATMVVD LIDEMEMKRV IERLGTLPVR GSTVNGEPCV PGCCAPRRRP
AASQTNPNAD APVASRS