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Entry: A0A0W7X178_9ACTN
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ID   A0A0W7X178_9ACTN        Unreviewed;       239 AA.
AC   A0A0W7X178;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Coproheme decarboxylase {ECO:0000256|HAMAP-Rule:MF_02244};
DE            EC=1.3.98.5 {ECO:0000256|HAMAP-Rule:MF_02244};
DE   AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000256|HAMAP-Rule:MF_02244};
DE   AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000256|HAMAP-Rule:MF_02244};
GN   Name=chdC {ECO:0000256|HAMAP-Rule:MF_02244};
GN   ORFNames=AT728_12275 {ECO:0000313|EMBL:KUF16546.1};
OS   Streptomyces silvensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF16546.1, ECO:0000313|Proteomes:UP000054804};
RN   [1] {ECO:0000313|EMBL:KUF16546.1, ECO:0000313|Proteomes:UP000054804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF16546.1,
RC   ECO:0000313|Proteomes:UP000054804};
RA   Johnston C.W., Li Y., Magarvey N.A.;
RT   "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT   novel hormone antagonists.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_02244}.
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:0000256|HAMAP-
CC         Rule:MF_02244};
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:0000256|HAMAP-
CC         Rule:MF_02244};
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:0000256|HAMAP-Rule:MF_02244};
CC   -!- COFACTOR:
CC       Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02244};
CC       Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC       {ECO:0000256|HAMAP-Rule:MF_02244};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02244}.
CC   -!- SIMILARITY: Belongs to the ChdC family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02244}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF16546.1}.
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DR   EMBL; LOCL01000038; KUF16546.1; -; Genomic_DNA.
DR   RefSeq; WP_058849364.1; NZ_LOCL01000038.1.
DR   AlphaFoldDB; A0A0W7X178; -.
DR   STRING; 1765722.AT728_12275; -.
DR   OrthoDB; 9773646at2; -.
DR   Proteomes; UP000054804; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016634; F:oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0006785; P:heme B biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02244; Coproheme_decarbox_2; 1.
DR   InterPro; IPR010644; ChdC/CLD.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   PANTHER; PTHR36843:SF1; COPROHEME DECARBOXYLASE; 1.
DR   PANTHER; PTHR36843; HEME-DEPENDENT PEROXIDASE YWFI-RELATED; 1.
DR   Pfam; PF06778; Chlor_dismutase; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_02244};
KW   Heme biosynthesis {ECO:0000256|HAMAP-Rule:MF_02244};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02244};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02244}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054804}.
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02244"
FT   BINDING         164
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:0000256|HAMAP-Rule:MF_02244"
SQ   SEQUENCE   239 AA;  27694 MW;  92DF1F7E9F0BD915 CRC64;
     MSDEASAKIP NAGKKAKDLN EVIRYTLWSV FKLRDVLPED RAGYADEVQE LFDKLAARDV
     TVRGTYDVSG LRADADVMIW WHAETADELQ EAYNLFRRTR LGRALEPVWS NMALHRPAEF
     NKSHIPAFLA DETPRDYVSV YPFVRSYDWY LLPDEDRRRM LADHGKMARG YPDVRANTVA
     SFSLGDYEWL LAFEADELYR IVDLMRHLRA SEARMHVREE VPFYTGRRKS VAELVATLA
//
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