CHDC_STAA8
ID CHDC_STAA8 Reviewed; 250 AA.
AC Q2G0J1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000303|PubMed:27597779};
DE EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:25908396};
DE AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305};
DE AltName: Full=Fe-coproporphyrin III oxidase/dehydrogenase {ECO:0000303|PubMed:25908396};
DE AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305};
GN Name=chdC {ECO:0000255|HAMAP-Rule:MF_01442};
GN Synonyms=hemQ {ECO:0000303|PubMed:25908396};
GN OrderedLocusNames=SAOUHSC_00573;
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, COFACTOR, AND PATHWAY.
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).
RN [3]
RP FUNCTION.
RX PubMed=27597779; DOI=10.1042/bcj20160696;
RA Hobbs C., Dailey H.A., Shepherd M.;
RT "The HemQ coprohaem decarboxylase generates reactive oxygen species:
RT implications for the evolution of classical haem biosynthesis.";
RL Biochem. J. 473:3997-4009(2016).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:25908396). Catalyzes the decarboxylation of Fe-coproporphyrin
CC III (coproheme) to heme b (protoheme IX), the last step of the pathway
CC (By similarity). The reaction occurs in a stepwise manner with a three-
CC propionate harderoheme intermediate (By similarity). Can stimulate the
CC generation of protoporphyrin IX, but not coproporphyrin III, by HemY
CC (PubMed:27597779). {ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:25908396, ECO:0000269|PubMed:27597779}.
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, ECO:0000269|PubMed:25908396};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:25908396};
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 ECO:0000269|PubMed:25908396};
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 ECO:0000269|PubMed:25908396};
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 (By similarity). Was originally thought to use heme as a cofactor
CC (PubMed:25908396). {ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:25908396};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000305|PubMed:25908396}.
CC -!- SIMILARITY: Belongs to the ChdC family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305}.
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DR EMBL; CP000253; ABD29716.1; -; Genomic_DNA.
DR RefSeq; WP_000075703.1; NZ_LS483365.1.
DR RefSeq; YP_499141.1; NC_007795.1.
DR AlphaFoldDB; Q2G0J1; -.
DR SMR; Q2G0J1; -.
DR STRING; 1280.SAXN108_0643; -.
DR EnsemblBacteria; ABD29716; ABD29716; SAOUHSC_00573.
DR GeneID; 3920614; -.
DR KEGG; sao:SAOUHSC_00573; -.
DR PATRIC; fig|93061.5.peg.516; -.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_063226_1_0_9; -.
DR OMA; RYTMWSV; -.
DR UniPathway; UPA00252; -.
DR PRO; PR:Q2G0J1; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW Heme; Heme biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..250
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000294046"
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; 29390 MW; B991C3DB917160E0 CRC64;
MSQAAETLDG WYSLHLFYAV DWASLRIVPK DERDALVTEF QSFLENTATV RSSKSGDQAI
YNITGQKADL LLWFLRPEMK SLNHIENEFN KLRIADFLIP TYSYVSVIEL SNYLAGKSDE
DPYENPHIKA RLYPELPHSD YICFYPMNKR RNETYNWYML TMEERQKLMY DHGMIGRKYA
GKIKQFITGS VGFDDFEWGV TLFSDDVLQF KKIVYEMRFD ETTARYGEFG SFFVGHIINT
NEFDQFFAIS
