CHDC_STAAR
ID CHDC_STAAR Reviewed; 250 AA.
AC Q6GJ81;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=SAR0593;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39613.1; -; Genomic_DNA.
DR RefSeq; WP_000075713.1; NC_002952.2.
DR AlphaFoldDB; Q6GJ81; -.
DR SMR; Q6GJ81; -.
DR KEGG; sar:SAR0593; -.
DR HOGENOM; CLU_063226_1_0_9; -.
DR OMA; RYTMWSV; -.
DR OrthoDB; 1616312at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000000596; 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..250
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000294051"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 131
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 145..149
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 172
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 185
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
SQ SEQUENCE 250 AA; 29389 MW; 8CF5959DE5162875 CRC64;
MSQAAETLDG WYSLHLFYAV DWASLRLVPK DERDALVTEF QSFLENTATV RSSKSGDQAI
YNITGQKADL LLWFLRPEMK SLNHIENEFN KLRIADFLIP TYSYVSVIEL SNYLAGKSDE
DPYENPHIKA RLYPELPHSD YICFYPMNKR RNETYNWYML TMEERQKLMY DHGMIGRKYA
GKIKQFITGS VGFDDFEWGV TLFSDDVLQF KKIVYEMRFD ETTARYGEFG SFFVGHIINT
NEFNQFFAIS
