CPFC_STAA8
ID CPFC_STAA8 Reviewed; 307 AA.
AC Q2FXA4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Coproporphyrin III ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000303|PubMed:25908396};
DE EC=4.99.1.9 {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:25908396};
GN Name=cpfC {ECO:0000250|UniProtKB:P32396, ECO:0000255|HAMAP-Rule:MF_00323};
GN Synonyms=hemH {ECO:0000303|PubMed:25908396};
GN OrderedLocusNames=SAOUHSC_01961 {ECO:0000312|EMBL:ABD31022.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=25908396; DOI=10.1111/mmi.13041;
RA Lobo S.A., Scott A., Videira M.A., Winpenny D., Gardner M., Palmer M.J.,
RA Schroeder S., Lawrence A.D., Parkinson T., Warren M.J., Saraiva L.M.;
RT "Staphylococcus aureus haem biosynthesis: characterisation of the enzymes
RT involved in final steps of the pathway.";
RL Mol. Microbiol. 97:472-487(2015).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:25908396). Catalyzes the insertion of ferrous iron into
CC coproporphyrin III to form Fe-coproporphyrin III (PubMed:25908396). It
CC can also insert iron into protoporphyrin IX, but it has a much stronger
CC preference for coproprophyrin III as the substrate (PubMed:25908396).
CC {ECO:0000269|PubMed:25908396}.
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 ECO:0000269|PubMed:25908396};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323,
CC ECO:0000269|PubMed:25908396};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for Fe(2+) (in the presence of coproporphyrin III)
CC {ECO:0000269|PubMed:25908396};
CC KM=52 uM for Fe(2+) (in the presence of protoporphyrin IX)
CC {ECO:0000269|PubMed:25908396};
CC Note=kcat is 165 min(-1) with coproporphyrin III as substrate. kcat
CC is 15 min(-1) with protoporphyrin IX as substrate.
CC {ECO:0000269|PubMed:25908396};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00323,
CC ECO:0000269|PubMed:25908396}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- DISRUPTION PHENOTYPE: Mutant accumulates coproporphyrin III.
CC {ECO:0000269|PubMed:25908396}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC Rule:MF_00323, ECO:0000305}.
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DR EMBL; CP000253; ABD31022.1; -; Genomic_DNA.
DR RefSeq; WP_000162880.1; NZ_LS483365.1.
DR RefSeq; YP_500460.1; NC_007795.1.
DR AlphaFoldDB; Q2FXA4; -.
DR SMR; Q2FXA4; -.
DR STRING; 1280.SAXN108_1862; -.
DR EnsemblBacteria; ABD31022; ABD31022; SAOUHSC_01961.
DR GeneID; 3920906; -.
DR KEGG; sao:SAOUHSC_01961; -.
DR PATRIC; fig|93061.5.peg.1786; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_2_1_9; -.
DR OMA; LGDPYHC; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..307
FT /note="Coproporphyrin III ferrochelatase"
FT /id="PRO_0000450325"
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 181
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P32396, ECO:0000255|HAMAP-
FT Rule:MF_00323"
FT BINDING 263
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P32396, ECO:0000255|HAMAP-
FT Rule:MF_00323"
SQ SEQUENCE 307 AA; 35070 MW; F8EB332969C45043 CRC64;
MTKKMGLLVM AYGTPYKESD IEPYYTDIRH GKRPSEEELQ DLKDRYEFIG GLSPLAGTTD
DQADALVSAL NKAYADVEFK LYLGLKHISP FIEDAVEQMH NDGITEAITV VLAPHYSSFS
VGSYDKRADE EAAKYGIQLT HVKHYYEQPK FIEYWTNKVN ETLAQIPEEE HKDTVLVVSA
HSLPKGLIEK NNDPYPQELE HTALLIKEQS NIEHIAIGWQ SEGNTGTPWL GPDVQDLTRD
LYEKHQYKNF IYTPVGFVCE HLEVLYDNDY ECKVVCDDIG ANYYRPKMPN THPLFIGAII
DEIKSIF
