CHDC_STAAE
ID CHDC_STAAE Reviewed; 250 AA.
AC A6QEP0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305};
DE EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566};
DE AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305};
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:23737523}; OrderedLocusNames=NWMN_0550;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP FUNCTION, COFACTOR, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=Newman;
RX PubMed=23737523; DOI=10.1074/jbc.m112.442335;
RA Mayfield J.A., Hammer N.D., Kurker R.C., Chen T.K., Ojha S., Skaar E.P.,
RA DuBois J.L.;
RT "The chlorite dismutase (HemQ) from Staphylococcus aureus has a redox-
RT sensitive heme and is associated with the small colony variant phenotype.";
RL J. Biol. Chem. 288:23488-23504(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26083961; DOI=10.1021/acs.biochem.5b00492;
RA Celis A.I., Streit B.R., Moraski G.C., Kant R., Lash T.D.,
RA Lukat-Rodgers G.S., Rodgers K.R., DuBois J.L.;
RT "Unusual peroxide-dependent, heme-transforming reaction catalyzed by
RT HemQ.";
RL Biochemistry 54:4022-4032(2015).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, AND MUTAGENESIS OF
RP TYR-113; ARG-131; TYR-145; LYS-149; TRP-157; GLN-185; TRP-198 AND ARG-218.
RX PubMed=27936663; DOI=10.1021/jacs.6b11324;
RA Celis A.I., Gauss G.H., Streit B.R., Shisler K., Moraski G.C.,
RA Rodgers K.R., Lukat-Rodgers G.S., Peters J.W., DuBois J.L.;
RT "Structure-based mechanism for oxidative decarboxylation reactions mediated
RT by amino acids and heme propionates in coproheme decarboxylase (HemQ).";
RL J. Am. Chem. Soc. 139:1900-1911(2017).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27982566; DOI=10.1021/acs.biochem.6b00958;
RA Streit B.R., Celis A.I., Shisler K., Rodgers K.R., Lukat-Rodgers G.S.,
RA DuBois J.L.;
RT "Reactions of ferrous coproheme decarboxylase (HemQ) with O2 and H2O2 yield
RT ferric heme b.";
RL Biochemistry 56:189-201(2017).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:26083961). Catalyzes the decarboxylation of Fe-coproporphyrin
CC III (coproheme) to heme b (protoheme IX), the last step of the pathway
CC (PubMed:26083961, PubMed:27936663, PubMed:27982566). The reaction
CC occurs in a stepwise manner with a three-propionate harderoheme
CC intermediate (PubMed:26083961, PubMed:27936663, PubMed:27982566). The
CC first decarboxylation step is fast and yields the three-propionate
CC harderoheme isomer III intermediate, while the slower second
CC decarboxylation appears to control the overall rate. H(2)O(2) is the
CC assumed biological oxidant, but either H(2)O(2) or peracetic acid
CC yields the same intermediates and products (PubMed:26083961). Has weak
CC peroxidase and catalase activities in vitro (PubMed:23737523).
CC {ECO:0000269|PubMed:23737523, ECO:0000269|PubMed:26083961,
CC ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566}.
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:26083961,
CC ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663};
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, ECO:0000269|PubMed:26083961,
CC ECO:0000269|PubMed:27936663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663};
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 ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663};
CC -!- COFACTOR:
CC Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000305|PubMed:27936663};
CC Note=Fe-coproporphyrin III acts as both substrate and redox cofactor
CC (Probable). Was originally thought to use heme as a cofactor
CC (PubMed:23737523). {ECO:0000269|PubMed:23737523,
CC ECO:0000305|PubMed:27936663};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000305|PubMed:23737523, ECO:0000305|PubMed:26083961}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23737523}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant forms slow growing small colonies
CC under aerobic but not anaerobic conditions. Mutant accumulates
CC coproporphyrin specifically under aerobic conditions and shows
CC deficiencies in catalase activity and peroxide resistance.
CC {ECO:0000269|PubMed:23737523}.
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; AP009351; BAF66822.1; -; Genomic_DNA.
DR RefSeq; WP_000075703.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QEP0; -.
DR SMR; A6QEP0; -.
DR EnsemblBacteria; BAF66822; BAF66822; NWMN_0550.
DR KEGG; sae:NWMN_0550; -.
DR HOGENOM; CLU_063226_1_0_9; -.
DR OMA; RYTMWSV; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000006386; 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.
FT CHAIN 1..250
FT /note="Coproheme decarboxylase"
FT /id="PRO_1000073519"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442,
FT ECO:0000305|PubMed:27936663"
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"
FT MUTAGEN 113
FT /note="Y->S: Has little effect on activity."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 131
FT /note="R->A: Has little effect on activity."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 145
FT /note="Y->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 149
FT /note="K->A: Forms harderoheme III as major product with
FT relatively little turnover to heme b."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 157
FT /note="W->F: Has little effect on activity."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 185
FT /note="Q->A: Has little effect on activity. Does not
FT accumulate harderoheme III."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 198
FT /note="W->F: Has little effect on activity."
FT /evidence="ECO:0000269|PubMed:27936663"
FT MUTAGEN 218
FT /note="R->A: Has little effect on activity."
FT /evidence="ECO:0000269|PubMed:27936663"
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
