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CHDC_BACC3
ID   CHDC_BACC3              Reviewed;         247 AA.
AC   C1EQ58;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442};
DE            EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_01442};
DE   AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442};
DE   AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000255|HAMAP-Rule:MF_01442};
GN   Name=chdC {ECO:0000255|HAMAP-Rule:MF_01442}; OrderedLocusNames=BCA_5540;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to
CC       heme b (protoheme IX), the last step of the pathway. The reaction
CC       occurs in a stepwise manner with a three-propionate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_01442}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme
CC         b; Xref=Rhea:RHEA:56516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:68438; EC=1.3.98.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01442};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + H(+) + H2O2 = CO2 + 2 H2O +
CC         harderoheme III; Xref=Rhea:RHEA:57940, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:68438, ChEBI:CHEBI:142463; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01442};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O2 + harderoheme III = CO2 + 2 H2O + heme b;
CC         Xref=Rhea:RHEA:57944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:142463; Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC   -!- COFACTOR:
CC       Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC       Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC       {ECO:0000255|HAMAP-Rule:MF_01442};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442}.
CC   -!- SIMILARITY: Belongs to the ChdC family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01442}.
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DR   EMBL; CP001407; ACO28152.1; -; Genomic_DNA.
DR   RefSeq; WP_001287585.1; NZ_CP009318.1.
DR   AlphaFoldDB; C1EQ58; -.
DR   SMR; C1EQ58; -.
DR   EnsemblBacteria; ACO28152; ACO28152; BCA_5540.
DR   GeneID; 56655111; -.
DR   GeneID; 64200587; -.
DR   KEGG; bcx:BCA_5540; -.
DR   PATRIC; fig|572264.18.peg.5462; -.
DR   OMA; RYTMWSV; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000002210; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01442; Coproheme_decarbox_1; 1.
DR   InterPro; IPR031332; CHDC.
DR   InterPro; IPR010644; ChdC/CLD.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   PANTHER; PTHR36843; PTHR36843; 1.
DR   Pfam; PF06778; Chlor_dismutase; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
PE   3: Inferred from homology;
KW   Heme; Heme biosynthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..247
FT                   /note="Coproheme decarboxylase"
FT                   /id="PRO_1000184937"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT   BINDING         129
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT   BINDING         143..147
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT   BINDING         170
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_01442"
FT   BINDING         183
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT   BINDING         221
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
SQ   SEQUENCE   247 AA;  28652 MW;  6812123FC9B44C2D CRC64;
     MSEATTTLDG WYCLHDLRSI DWAAWKTLSS DERGQAVSEF LNVVEKWNDV AAAKKGSHAM
     YTVVGQKADI MLMILRPTME ELNEIETELN KTTLAEYMVP AYSYVSVVEL SNYLPADEDP
     YQNPQILARL YPELPKANHI CFYPMDKRRQ GDDNWYMLPM EERKKMMYSH SKIGRQYAGK
     VRQVISGSVG FDDFEWGVTL FADDVLQFKK LIYEMRFDEV SARYGEFGTF FVGNILPDEK
     VEKFLHI
 
 
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