CHDC_MYCTO
ID CHDC_MYCTO Reviewed; 231 AA.
AC P9WL44; L0TBY3; P71973; Q7D6S6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_02244};
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};
DE AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000255|HAMAP-Rule:MF_02244};
GN Name=chdC {ECO:0000255|HAMAP-Rule:MF_02244}; OrderedLocusNames=MT2750;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 -!- SIMILARITY: Belongs to the ChdC family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02244}.
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DR EMBL; AE000516; AAK47065.1; -; Genomic_DNA.
DR PIR; H70968; H70968.
DR RefSeq; WP_003413869.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WL44; -.
DR SMR; P9WL44; -.
DR EnsemblBacteria; AAK47065; AAK47065; MT2750.
DR KEGG; mtc:MT2750; -.
DR PATRIC; fig|83331.31.peg.2961; -.
DR HOGENOM; CLU_076582_1_0_11; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..231
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000427543"
FT ACT_SITE 133
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02244"
FT BINDING 156
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 231 AA; 26250 MW; F85C43F300CD9DA4 CRC64;
MARLDYDALN ATLRYLMFSV FSVSPGALGD QRDAIIDDAS TFFKQQEERG VVVRGLYDVA
GLRADADFMV WTHAERVEAL QATYADFRRT TTLGRACTPV WSGVGLHRPA EFNKSHIPAF
LAGEEPGAYI CVYPFVRSYE WYLLPDEERR RMLAEHGMAA RGYKDVRANT VPAFALGDYE
WILAFEAPEL DRIVDLMREL RATDARRHTR AETPFFTGPR VPVEQLVHSL P
