ID A0A147EP86_9MICO Unreviewed; 240 AA.
AC A0A147EP86;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=NS354_05735 {ECO:0000313|EMBL:KTR86194.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR86194.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR86194.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR86194.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR86194.1}.
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DR EMBL; LDRK01000026; KTR86194.1; -; Genomic_DNA.
DR RefSeq; WP_058593624.1; NZ_LDRK01000026.1.
DR AlphaFoldDB; A0A147EP86; -.
DR PATRIC; fig|1079994.3.peg.1239; -.
DR OrthoDB; 9773646at2; -.
DR Proteomes; UP000070810; 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:UP000070810}.
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 240 AA; 27224 MW; 7A75F5D6CF0D2E49 CRC64;
MNEGERPQVD HRHVAEQINA ATNFTMYAVF AERRGAEGER AGSPPGDVAE LLAALERIEG
LQTRGWYDIS GFRADADLLV WWFAPTTDAL QRAYRTLWEW GGGRLAPVWS NIGVHRAAEF
NRGHVPAFLA GDAPKEFLCV YPFVRGRDWY LLPDAERGKL LREHGMAARD YGDVLANTVA
SFALGDYEWL LAFEADDLVR IVDLMRELRA TEARRHVIEE TPFFTGPRRP AEELLLRIAR
//
