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CHDC_GEOTN
ID   CHDC_GEOTN              Reviewed;         248 AA.
AC   A4ITP5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
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=GTNG_3362;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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   -!- SIMILARITY: Belongs to the ChdC family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01442}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABO68699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000557; ABO68699.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035499495.1; NC_009328.1.
DR   AlphaFoldDB; A4ITP5; -.
DR   SMR; A4ITP5; -.
DR   STRING; 420246.GTNG_3362; -.
DR   EnsemblBacteria; ABO68699; ABO68699; GTNG_3362.
DR   KEGG; gtn:GTNG_3362; -.
DR   eggNOG; COG3253; Bacteria.
DR   HOGENOM; CLU_063226_1_0_9; -.
DR   OMA; RYTMWSV; -.
DR   OrthoDB; 1616312at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000001578; 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   3: Inferred from homology;
KW   Heme; Heme biosynthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..248
FT                   /note="Coproheme decarboxylase"
FT                   /id="PRO_0000294039"
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"
SQ   SEQUENCE   248 AA;  28865 MW;  9823B8F8357F2254 CRC64;
     MSEAAQTLDG WYCLHDFRTI DWSAWKMLPN EERQAAIDEF LALVDKWETT ESEQQGSHAI
     YTIVGQKADI LFMILRPTLD ELHEIETALN KTKLAEYLLP AYSYVSVVEL SNYLASGNED
     PYQIPEVRRR LYPILPKTNY ICFYPMDKRR QGDDNWYMLS MEQRRELMRA HGMTGRKYAG
     KVTQIITGSV GLDDFEWGVT LFSDDALQFK KLVYEMRFDE VSARFGEFGS FFVGNRLAAE
     NVPTFFHI
 
 
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