CPFC_LISMO
ID CPFC_LISMO Reviewed; 309 AA.
AC Q8Y565;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Coproporphyrin III ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000305};
DE EC=4.99.1.9 {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:31794133};
GN Name=cpfC {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000303|PubMed:31794133};
GN Synonyms=hemH; OrderedLocusNames=lmo2211;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2] {ECO:0007744|PDB:6RWV, ECO:0007744|PDB:6SV3}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP FE-COPROPORPHYRIN III, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=31794133; DOI=10.1111/febs.15164;
RA Hofbauer S., Helm J., Obinger C., Djinovic-Carugo K., Furtmueller P.G.;
RT "Crystal structures and calorimetry reveal catalytically relevant binding
RT mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.";
RL FEBS J. 287:2779-2796(2020).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:31794133). Catalyzes the insertion of ferrous iron into
CC coproporphyrin III to form Fe-coproporphyrin III (PubMed:31794133).
CC {ECO:0000269|PubMed:31794133}.
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:31794133};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323,
CC ECO:0000269|PubMed:31794133};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 uM for Fe(2+) {ECO:0000269|PubMed:31794133};
CC Note=kcat is 7.9 min(-1). {ECO:0000269|PubMed:31794133};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00323,
CC ECO:0000269|PubMed:31794133}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:31794133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC Rule:MF_00323, ECO:0000305}.
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DR EMBL; AL591982; CAD00289.1; -; Genomic_DNA.
DR PIR; AC1351; AC1351.
DR RefSeq; NP_465735.1; NC_003210.1.
DR RefSeq; WP_010989926.1; NZ_CP023861.1.
DR PDB; 6RWV; X-ray; 1.64 A; A=1-309.
DR PDB; 6SV3; X-ray; 1.64 A; A=1-309.
DR PDBsum; 6RWV; -.
DR PDBsum; 6SV3; -.
DR AlphaFoldDB; Q8Y565; -.
DR SMR; Q8Y565; -.
DR STRING; 169963.lmo2211; -.
DR PaxDb; Q8Y565; -.
DR EnsemblBacteria; CAD00289; CAD00289; CAD00289.
DR GeneID; 984632; -.
DR KEGG; lmo:lmo2211; -.
DR PATRIC; fig|169963.11.peg.2263; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_2_1_9; -.
DR OMA; LGDPYHC; -.
DR PhylomeDB; Q8Y565; -.
DR BioCyc; LMON169963:LMO2211-MON; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000000817; 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 3D-structure; Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..309
FT /note="Coproporphyrin III ferrochelatase"
FT /id="PRO_0000175161"
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 ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3"
FT BINDING 14
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323,
FT ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3"
FT BINDING 29
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323,
FT ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3"
FT BINDING 45..46
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323,
FT ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3"
FT BINDING 53
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323,
FT ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3"
FT BINDING 124
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323,
FT ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3"
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"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:6RWV"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 53..73
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 79..91
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:6RWV"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6RWV"
FT TURN 266..270
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:6RWV"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6RWV"
FT HELIX 293..309
FT /evidence="ECO:0007829|PDB:6RWV"
SQ SEQUENCE 309 AA; 35344 MW; 2CD5D34612217D6E CRC64;
MTKKVGLLVM AYGTPYKDED IERYYTDIRH GHKPSEEMIA DLRGRYHAIG GLSPLAKITE
AQAYGLEKAL NDSQDEVEFK AYIGLKHIEP FIEDAVEAMH KDGIEEAISI VLAPHYSSFS
VEAYNKRAKE AADKLGGPRI NAINDWYKQP KFIQMWADRI NETAKQIPAD ELLDTVLIVS
AHSLPEKIKQ HNDPYPNQLQ ETADFIFEKV VVPHYALGWQ SEGKTGEPWL GPDVQDLTRE
LYGREKYKHF IYTPVGFVAE HLEVLYDNDY ECKVVTDEVG AAYHRPPMPN SDPEFLEVLR
TVVWEKYSN
