CHDC_GEOS3
ID CHDC_GEOS3 Reviewed; 248 AA.
AC A0A0K2H9D8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000303|PubMed:27936663};
DE EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27936663};
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};
GN ORFNames=GT50_08830 {ECO:0000312|EMBL:ALA70306.1};
OS Geobacillus stearothermophilus (strain DSM 13240 / CIP 106956 / 10).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=272567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13240 / CIP 106956 / 10;
RA Lewis S.A., Clifton S.W., Najar F.Z., Roe B.A.;
RT "Complete genome Sequence of Geobacillus stearothermophilus strain 10, a
RT Yellowstone hot spring isolate.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5T2K}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP MANGANESE-COPROPORPHYRIN III, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RX PubMed=27936663; DOI=10.1021/jacs.6b11324;
RA Celis A.I., Gauss G.H., Streit B.R., Shisler K., Moraski G.C.,
RA Rodgers K.R., Lukat-Rodgers G.S., Peters J.W., DuBois J.L.;
RT "Structure-based mechanism for oxidative decarboxylation reactions mediated
RT by amino acids and heme propionates in coproheme decarboxylase (HemQ).";
RL J. Am. Chem. Soc. 139:1900-1911(2017).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:27936663). Catalyzes the decarboxylation of Fe-coproporphyrin
CC III (coproheme) to heme b (protoheme IX), the last step of the pathway
CC (PubMed:27936663). The reaction occurs in a stepwise manner with a
CC three-propionate harderoheme intermediate (PubMed:27936663).
CC {ECO:0000269|PubMed:27936663}.
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, ECO:0000269|PubMed:27936663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:27936663};
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, ECO:0000269|PubMed:27936663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:27936663};
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 ECO:0000269|PubMed:27936663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:27936663};
CC -!- COFACTOR:
CC Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000305|PubMed:27936663};
CC Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:27936663};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:27936663}.
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; CP008934; ALA70306.1; -; Genomic_DNA.
DR RefSeq; WP_053414189.1; NZ_CP008934.1.
DR PDB; 5T2K; X-ray; 1.80 A; A/B/C/D/E=1-248.
DR PDBsum; 5T2K; -.
DR AlphaFoldDB; A0A0K2H9D8; -.
DR SMR; A0A0K2H9D8; -.
DR EnsemblBacteria; ALA70306; ALA70306; GT50_08830.
DR KEGG; gse:GT50_08830; -.
DR PATRIC; fig|272567.8.peg.1802; -.
DR BRENDA; 1.3.98.5; 623.
DR UniPathway; UPA00252; -.
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.
FT CHAIN 1..248
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000450276"
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 ECO:0000305|PubMed:27936663"
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 144
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000305|PubMed:27936663"
FT BINDING 148
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000305|PubMed:27936663"
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 ECO:0000269|PubMed:27936663"
FT BINDING 184
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442,
FT ECO:0000305|PubMed:27936663"
FT BINDING 222
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442,
FT ECO:0000305|PubMed:27936663"
FT STRAND 7..20
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 30..52
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 98..112
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:5T2K"
FT TURN 177..181
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5T2K"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5T2K"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5T2K"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:5T2K"
SQ SEQUENCE 248 AA; 28787 MW; 1E27A733004508B1 CRC64;
MSEAAQTLDG WYCLHDFRTI DWSAWKTLPN EEREAAISEF LALVDQWETT ESEKQGSHAV
YTIVGQKADI LFMILRPTLD ELHEIETALN KTKLADYLLP AYSYVSVVEL SNYLASGSED
PYQIPEVRRR LYPILPKTNY ICFYPMDKRR QGNDNWYMLS MEQRRELMRA HGMTGRKYAG
KVTQIITGSV GLDDFEWGVT LFSDDALQFK KLVYEMRFDE VSARFGEFGS FFVGTRLPME
NVSSFFHV
