ID U5W816_9ACTN Unreviewed; 235 AA.
AC U5W816;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AFR_35165 {ECO:0000313|EMBL:AGZ45289.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45289.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ45289.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45289.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ45289.1; -; Genomic_DNA.
DR RefSeq; WP_023561625.1; NC_022657.1.
DR AlphaFoldDB; U5W816; -.
DR STRING; 1246995.AFR_35165; -.
DR KEGG; afs:AFR_35165; -.
DR PATRIC; fig|1246995.3.peg.7115; -.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_076582_1_0_11; -.
DR OrthoDB; 9773646at2; -.
DR Proteomes; UP000017746; Chromosome.
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:UP000017746}.
FT ACT_SITE 137
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02244"
FT BINDING 160
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 235 AA; 27088 MW; C96FC128FB81BF3B CRC64;
MTDQPQTNAA RVKELNATIR YTMWSVFKVA SPLPALREDL ASEVDALFEQ LLGKDVVVRG
TYDVSGLRAD ADILVWWHSE SPDALQEAYG LFRRTALGRH LEPVWSQMAL HRPAEFNKSH
LPAFLAGEEA RPYICVYPFV RSYEWYLLPD EERRFMLAEH GKMARGYPDV RANTVASFAL
GDYEWMLAFE ADELHRIVDL MRDLRASTAR RHVREEVPFY TGRRRSVTEL VATLP
//
