CHDC_THET8
ID CHDC_THET8 Reviewed; 249 AA.
AC Q5SHL6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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};
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}; OrderedLocusNames=TTHA1714;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), SUBUNIT, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=15965735; DOI=10.1007/s10969-005-1103-x;
RA Ebihara A., Okamoto A., Kousumi Y., Yamamoto H., Masui R., Ueyama N.,
RA Yokoyama S., Kuramitsu S.;
RT "Structure-based functional identification of a novel heme-binding protein
RT from Thermus thermophilus HB8.";
RL J. Struct. Funct. Genomics 6:21-32(2005).
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 harderoheme
CC intermediate (By similarity). When reconstituted with heme, can
CC generate oxygen using chlorite or hydrogen peroxide as substrate (in
CC vitro), but has very low affinity for hydrogen peroxide and chlorite
CC and extremely low enzyme activity (PubMed:15965735).
CC {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:15965735}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
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 -!- 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 -!- 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:15965735). {ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:15965735};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 mM for chlorite {ECO:0000269|PubMed:15965735};
CC KM=25 mM for hydrogen peroxide {ECO:0000269|PubMed:15965735};
CC Note=kcat is 0.77 sec(-1) with chlorite and 0.52 sec(-1) with
CC hydrogen peroxide. The kcat values are at least 1000 times lower than
CC those observed for well-characterized chlorite dismutases, and the
CC specific activity is even lower.;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:15965735}.
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; AP008226; BAD71537.1; -; Genomic_DNA.
DR RefSeq; WP_011173736.1; NC_006461.1.
DR RefSeq; YP_144980.1; NC_006461.1.
DR PDB; 1VDH; X-ray; 2.00 A; A/B/C/D/E=1-249.
DR PDBsum; 1VDH; -.
DR AlphaFoldDB; Q5SHL6; -.
DR SMR; Q5SHL6; -.
DR STRING; 300852.55773096; -.
DR EnsemblBacteria; BAD71537; BAD71537; BAD71537.
DR GeneID; 3169367; -.
DR KEGG; ttj:TTHA1714; -.
DR PATRIC; fig|300852.9.peg.1684; -.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_063226_1_0_0; -.
DR OMA; RYTMWSV; -.
DR PhylomeDB; Q5SHL6; -.
DR UniPathway; UPA00252; -.
DR EvolutionaryTrace; Q5SHL6; -.
DR Proteomes; UP000000532; 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 3D-structure; Heme; Heme biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..249
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000294059"
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"
FT BINDING 223
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT STRAND 10..24
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 34..56
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 102..119
FT /evidence="ECO:0007829|PDB:1VDH"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:1VDH"
FT TURN 178..182
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1VDH"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1VDH"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1VDH"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:1VDH"
SQ SEQUENCE 249 AA; 28906 MW; 2F06D2269ACBD9D6 CRC64;
MERHVPEPTH TLEGWHVLHD FRLLDFARWF SAPLEAREDA WEELKGLVRE WRELEEAGQG
SYGIYQVVGH KADLLFLNLR PGLDPLLEAE ARLSRSAFAR YLGRSYSFYS VVELGSQEKP
LDPESPYVKP RLTPRVPKSG YVCFYPMNKR RQGQDNWYML PAKERASLMK AHGETGRKYQ
GKVMQVISGA QGLDDWEWGV DLFSEDPVQF KKIVYEMRFD EVSARYGEFG PFFVGKYLDE
EALRAFLGL
