CHDC_GEOKA
ID CHDC_GEOKA Reviewed; 248 AA.
AC Q5KUD5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442};
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};
DE AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000255|HAMAP-Rule:MF_01442};
GN Name=chdC {ECO:0000255|HAMAP-Rule:MF_01442}; OrderedLocusNames=GK3416;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of APC35880 protein from Bacillus stearothermophilus.";
RL Submitted (APR-2004) to the PDB data bank.
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_01442}.
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 {ECO:0000255|HAMAP-Rule:MF_01442};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the ChdC family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01442}.
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DR EMBL; BA000043; BAD77701.1; -; Genomic_DNA.
DR RefSeq; WP_011232883.1; NC_006510.1.
DR PDB; 1T0T; X-ray; 1.75 A; V/W/X/Y/Z=1-248.
DR PDBsum; 1T0T; -.
DR AlphaFoldDB; Q5KUD5; -.
DR SMR; Q5KUD5; -.
DR STRING; 235909.GK3416; -.
DR EnsemblBacteria; BAD77701; BAD77701; GK3416.
DR KEGG; gka:GK3416; -.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_063226_1_0_9; -.
DR OMA; RYTMWSV; -.
DR UniPathway; UPA00252; -.
DR EvolutionaryTrace; Q5KUD5; -.
DR Proteomes; UP000001172; 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..248
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000294038"
FT ACT_SITE 144
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 130
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 144..148
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 171
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 184
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 222
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT STRAND 8..20
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 30..52
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 98..110
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:1T0T"
FT TURN 177..181
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1T0T"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1T0T"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1T0T"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:1T0T"
SQ SEQUENCE 248 AA; 28769 MW; 5F3A13FC0047D8B6 CRC64;
MSEAAQTLDG WYCLHDFRTI DWSAWKTLPN EEREAAISEF LALVDQWETT ESEKQGSHAV
YTIVGQKADI LFMILRPTLD ELHEIETALN KTKLADYLLP AYSYVSVVEL SNYLASGSED
PYQIPEVRRR LYPILPKTNY ICFYPMDKRR QGNDNWYMLS MEQRRELMRA HGMTGRKYAG
KVTQIITGSV GLDDFEWGVT LFSDDALQFK KLVYEMRFDE VSARFGEFGS FFVGTRLSVE
KVPSFFHV
