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CHDC_ALKHC
ID   CHDC_ALKHC              Reviewed;         249 AA.
AC   Q9K6A4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
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=BH3825;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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=BAB07544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000004; BAB07544.1; ALT_INIT; Genomic_DNA.
DR   PIR; A84128; A84128.
DR   RefSeq; WP_010899950.1; NC_002570.2.
DR   AlphaFoldDB; Q9K6A4; -.
DR   SMR; Q9K6A4; -.
DR   STRING; 272558.10176450; -.
DR   EnsemblBacteria; BAB07544; BAB07544; BAB07544.
DR   KEGG; bha:BH3825; -.
DR   eggNOG; COG3253; Bacteria.
DR   HOGENOM; CLU_063226_1_0_9; -.
DR   OMA; RYTMWSV; -.
DR   OrthoDB; 1616312at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000001258; 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;
KW   Reference proteome.
FT   CHAIN           1..249
FT                   /note="Coproheme decarboxylase"
FT                   /id="PRO_0000294034"
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"
SQ   SEQUENCE   249 AA;  28942 MW;  8841E34258E175CE CRC64;
     MNEAAKTLDG WYCLHDFRTI NWAELKTLST EERQQIINEF LDLMEKWNDT EAQGEGSHAV
     YTIVGQKADV MLMILRPSME ELNEIETAFN KSRFAEFTVP AYSYVSVVEL SNYMAGDSDD
     DPYQNPHVRA RLYPQLPKAK HVCFYPMDKR RQGDDNWYML PMDQRRELMK SHGMIGRSYA
     GKVKQIITGS VGFDDWEWGV TLFADDVLQF KKLVYEMRFD EVSARYGEFG SFFVGNLLTA
     EGIPSYFYV
 
 
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