ID A0A160KQ26_9MICO Unreviewed; 259 AA.
AC A0A160KQ26;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=A6122_0402 {ECO:0000313|EMBL:AND15562.1}, C5C18_12185
GN {ECO:0000313|EMBL:PPG05779.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND15562.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND15562.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND15562.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPG05779.1, ECO:0000313|Proteomes:UP000239776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSPB 2748 {ECO:0000313|EMBL:PPG05779.1,
RC ECO:0000313|Proteomes:UP000239776};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; CP015515; AND15562.1; -; Genomic_DNA.
DR EMBL; PSUO01000022; PPG05779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160KQ26; -.
DR STRING; 33888.A6122_0402; -.
DR KEGG; rtn:A6122_0402; -.
DR PATRIC; fig|33888.3.peg.456; -.
DR OrthoDB; 9773646at2; -.
DR Proteomes; UP000077071; Chromosome.
DR Proteomes; UP000239776; 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:UP000077071}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02244"
FT BINDING 184
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 259 AA; 29107 MW; BFC486B8EE56D389 CRC64;
MIDQTAGTAD PVQSAPDTSA AVAAPQLPAD QDHSDQALGY TLWAVLRRDP ARPFTLSSDA
VAPAVKQYEH LVAQLDGGGV TVRGTYDVSA LRADADIMLW LTGSAPEELQ RAYREVRRSE
LLVGLLPTWN AMGVHRDAEF SANHLPAYMR GKAPARWLTV YPFVRSYEWY ILPEEERRAM
LAQHGRQGSR FRSVLTNTVA SFSLGDYEWI LALEDEELVN LVDLMRDLRA TEARRHVREE
VPFYTGRRIE ADQIAEVLR
//
