CHDC_MYCTU
ID CHDC_MYCTU Reviewed; 231 AA.
AC P9WL45; 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, ECO:0000303|PubMed:25646457};
DE EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_02244, ECO:0000269|PubMed:25646457};
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};
DE AltName: Full=Iron-coproporphyrin oxidative decarboxylase {ECO:0000303|PubMed:25711532};
GN Name=chdC {ECO:0000255|HAMAP-Rule:MF_02244, ECO:0000303|PubMed:28123057};
GN Synonyms=hemQ {ECO:0000303|PubMed:20543190}; OrderedLocusNames=Rv2676c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-44, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP COFACTOR, PATHWAY, AND MUTAGENESIS OF HIS-156.
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=25646457; DOI=10.1073/pnas.1416285112;
RA Dailey H.A., Gerdes S., Dailey T.A., Burch J.S., Phillips J.D.;
RT "Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway
RT that does not use protoporphyrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:2210-2215(2015).
RN [6]
RP PATHWAY, AND REVIEW.
RX PubMed=25711532; DOI=10.1016/j.abb.2015.02.017;
RA Dailey H.A., Gerdes S.;
RT "HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme
RT synthesis in Firmicutes and Actinobacteria.";
RL Arch. Biochem. Biophys. 574:27-35(2015).
RN [7]
RP NOMENCLATURE, AND REVIEW.
RX PubMed=28123057; DOI=10.1128/mmbr.00048-16;
RA Dailey H.A., Dailey T.A., Gerdes S., Jahn D., Jahn M., O'Brian M.R.,
RA Warren M.J.;
RT "Prokaryotic heme biosynthesis: multiple pathways to a common essential
RT product.";
RL Microbiol. Mol. Biol. Rev. 81:e00048-e00048(2017).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:25646457). Catalyzes the decarboxylation of Fe-coproporphyrin
CC III (coproheme) to heme b (protoheme IX), the last step of the pathway
CC (PubMed:25646457). The reaction occurs in a stepwise manner with a
CC three-propionate intermediate (By similarity).
CC {ECO:0000250|UniProtKB:Q8Y5F1, ECO:0000269|PubMed:25646457}.
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, ECO:0000269|PubMed:25646457};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02244,
CC ECO:0000269|PubMed:25646457};
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;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1, ECO:0000255|HAMAP-
CC Rule:MF_02244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1, ECO:0000255|HAMAP-
CC 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:0000250|UniProtKB:Q8Y5F1,
CC ECO:0000255|HAMAP-Rule:MF_02244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1, ECO:0000255|HAMAP-
CC Rule:MF_02244};
CC -!- COFACTOR:
CC Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1,
CC ECO:0000255|HAMAP-Rule:MF_02244};
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:20543190). {ECO:0000250|UniProtKB:Q8Y5F1,
CC ECO:0000269|PubMed:20543190};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02244,
CC ECO:0000269|PubMed:20543190, ECO:0000269|PubMed:25646457,
CC ECO:0000305|PubMed:25711532}.
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; AL123456; CCP45474.1; -; Genomic_DNA.
DR PIR; H70968; H70968.
DR RefSeq; NP_217192.1; NC_000962.3.
DR RefSeq; WP_003413869.1; NZ_NVQJ01000017.1.
DR AlphaFoldDB; P9WL45; -.
DR SMR; P9WL45; -.
DR STRING; 83332.Rv2676c; -.
DR PaxDb; P9WL45; -.
DR PRIDE; P9WL45; -.
DR DNASU; 887718; -.
DR GeneID; 887718; -.
DR KEGG; mtu:Rv2676c; -.
DR TubercuList; Rv2676c; -.
DR eggNOG; COG3253; Bacteria.
DR OMA; RYTMWSV; -.
DR PhylomeDB; P9WL45; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW Heme; Heme biosynthesis; Iron; Isopeptide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Ubl conjugation.
FT CHAIN 1..231
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000396082"
FT ACT_SITE 133
FT /evidence="ECO:0000250|UniProtKB:Q8Y5F1, ECO:0000255|HAMAP-
FT 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,
FT ECO:0000305|PubMed:20543190"
FT CROSSLNK 44
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT MUTAGEN 156
FT /note="H->A,C: Strong decrease in heme binding."
FT /evidence="ECO:0000269|PubMed:20543190"
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
