CHDC_STRCO
ID CHDC_STRCO Reviewed; 243 AA.
AC O69830;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_02244, ECO:0000305};
DE EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_02244};
DE AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000255|HAMAP-Rule:MF_02244, ECO:0000305};
DE AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000255|HAMAP-Rule:MF_02244, ECO:0000305};
GN Name=chdC {ECO:0000255|HAMAP-Rule:MF_02244};
GN OrderedLocusNames=SCO6042 {ECO:0000312|EMBL:CAA18976.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP PATHWAY.
RX PubMed=20543190; DOI=10.1074/jbc.m110.142604;
RA Dailey T.A., Boynton T.O., Albetel A.N., Gerdes S., Johnson M.K.,
RA Dailey H.A.;
RT "Discovery and characterization of HemQ: an essential heme biosynthetic
RT pathway component.";
RL J. Biol. Chem. 285:25978-25986(2010).
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_02244}.
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_02244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02244};
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_02244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02244};
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_02244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02244};
CC -!- COFACTOR:
CC Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02244};
CC Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC {ECO:0000255|HAMAP-Rule:MF_02244};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02244,
CC ECO:0000269|PubMed:20543190}.
CC -!- SIMILARITY: Belongs to the ChdC family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02244, ECO:0000305}.
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DR EMBL; AL939126; CAA18976.1; -; Genomic_DNA.
DR PIR; T34680; T34680.
DR RefSeq; NP_630152.1; NC_003888.3.
DR RefSeq; WP_003972879.1; NZ_VNID01000009.1.
DR AlphaFoldDB; O69830; -.
DR SMR; O69830; -.
DR STRING; 100226.SCO6042; -.
DR GeneID; 1101483; -.
DR KEGG; sco:SCO6042; -.
DR PATRIC; fig|100226.15.peg.6143; -.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_076582_1_0_11; -.
DR InParanoid; O69830; -.
DR OMA; RYTMWSV; -.
DR PhylomeDB; O69830; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_02244; Coproheme_decarbox_2; 1.
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;
KW Reference proteome.
FT CHAIN 1..243
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000450277"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02244"
FT BINDING 168
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_02244"
SQ SEQUENCE 243 AA; 28132 MW; 6180412A99FD8E04 CRC64;
MSDDASTPAA ERIPNKGKLA KDLNEVIRYT LWSVFKLKDT LPEDRAGYAD EVQELFDQLA
AKDVTIRGTY DLSGLRADAD LMIWWHAETA DQLQEAYNLF RRTKLGRALE PVWSNMALHR
PAEFNRSHIP AFLADETPRN YISVYPFVRS YDWYLLPDED RRRMLADHGK MARGYPDVRA
NTVASFSLGD YEWILAFEAD ELHRIVDLMR HLRGSEARRH VREEIPFYTG RRKDIGELVA
GLA
