CPFCB_CUTAK
ID CPFCB_CUTAK Reviewed; 683 AA.
AC P0DTW0; Q6AB01;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Coproporphyrin-dependent heme b biosynthesis bifunctional protein {ECO:0000305};
DE Includes:
DE RecName: Full=Coproporphyrin III ferrochelatase {ECO:0000250|UniProtKB:P9WNE3};
DE EC=4.99.1.9 {ECO:0000250|UniProtKB:P9WNE3};
DE Includes:
DE RecName: Full=Coproheme decarboxylase {ECO:0000250|UniProtKB:Q8Y5F1};
DE EC=1.3.98.5 {ECO:0000250|UniProtKB:Q8Y5F1};
GN OrderedLocusNames=PPA0308;
GN ORFNames=cbac_01720 {ECO:0000312|EMBL:QAZ50313.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RA Deptula P., Laine P., Smolander O.-P., Paulin L., Auvinen P., Varmanen P.;
RT "PacBio re-sequencing of the Cutibacterium acnes strains DSM 16379 and DSM
RT 1897.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PATHWAY.
RX PubMed=20543190; DOI=10.1074/jbc.m110.142604;
RA Dailey T.A., Boynton T.O., Albetel A.N., Gerdes S., Johnson M.K.,
RA Dailey H.A.;
RT "Discovery and characterization of HemQ: an essential heme biosynthetic
RT pathway component.";
RL J. Biol. Chem. 285:25978-25986(2010).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=25646457; DOI=10.1073/pnas.1416285112;
RA Dailey H.A., Gerdes S., Dailey T.A., Burch J.S., Phillips J.D.;
RT "Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway
RT that does not use protoporphyrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:2210-2215(2015).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:25646457). Catalyzes the insertion of ferrous iron into
CC coproporphyrin III to form coproheme III (By similarity). Also
CC catalyzes the decarboxylation of coproheme III to heme b (protoheme
CC IX), the last step of the pathway (By similarity).
CC {ECO:0000250|UniProtKB:P9WNE3, ECO:0000250|UniProtKB:Q8Y5F1,
CC ECO:0000269|PubMed:25646457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+);
CC Xref=Rhea:RHEA:49572, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:68438, ChEBI:CHEBI:131725; EC=4.99.1.9;
CC Evidence={ECO:0000250|UniProtKB:P9WNE3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574;
CC Evidence={ECO:0000250|UniProtKB:P9WNE3};
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;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1};
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;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1};
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:0000250|UniProtKB:Q8Y5F1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1};
CC -!- COFACTOR:
CC Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC Evidence={ECO:0000250|UniProtKB:Q8Y5F1};
CC Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC {ECO:0000250|UniProtKB:Q8Y5F1};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:20543190,
CC ECO:0000269|PubMed:25646457}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ferrochelatase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ChdC family.
CC {ECO:0000305}.
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DR EMBL; AE017283; AAT82065.1; -; Genomic_DNA.
DR EMBL; CP025935; QAZ50313.1; -; Genomic_DNA.
DR RefSeq; WP_002517081.1; NZ_CP025935.1.
DR AlphaFoldDB; P0DTW0; -.
DR SMR; P0DTW0; -.
DR STRING; 267747.PPA0308; -.
DR EnsemblBacteria; AAT82065; AAT82065; PPA0308.
DR KEGG; pac:PPA0308; -.
DR PATRIC; fig|267747.3.peg.319; -.
DR eggNOG; COG0276; Bacteria.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_024568_0_0_11; -.
DR OMA; VMKDLRY; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000000603; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
DR HAMAP; MF_00323; Ferrochelatase; 1.
DR InterPro; IPR010644; ChdC/CLD.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF06778; Chlor_dismutase; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR00109; hemH; 1.
PE 3: Inferred from homology;
KW Heme; Heme biosynthesis; Iron; Lyase; Metal-binding; Oxidoreductase;
KW Porphyrin biosynthesis.
FT CHAIN 1..683
FT /note="Coproporphyrin-dependent heme b biosynthesis
FT bifunctional protein"
FT /id="PRO_0000450326"
FT REGION 1..330
FT /note="Coproporphyrin III ferrochelatase"
FT /evidence="ECO:0000305"
FT REGION 382..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..683
FT /note="Coproheme decarboxylase"
FT /evidence="ECO:0000305"
FT ACT_SITE 583
FT /note="For coproheme decarboxylase activity"
FT /evidence="ECO:0000250|UniProtKB:Q8Y5F1"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32396"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32396"
FT BINDING 606
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:0000250|UniProtKB:Q8Y5F1"
SQ SEQUENCE 683 AA; 74065 MW; 8E27CFA6BA620B00 CRC64;
MTANPYAAPT DPLAPYSAVL VVSFGGPRSP EEVMPFLRRV SHGRIPEERL ADVARHYDRF
GGVSPINDAT DVFVNAIGNE LRRHGVRVPV LLGNRNGTPF LEEALTDMHA HGVRRVLAVV
TSAYASYSGC RQYREEIATA LAHAGITDMQ VDKVPPFNEA PGFIRANAEA LMQAFMRIPP
TPLEATRVVF VTHSIPDSMQ DASGAGQPGT DYISQHKAVC ERVAGQVRQV FGNMPQWDLA
YCSRSGRPSD PWLEPDIIDH LRSLPEQGVQ SVVVAPIGFV ADHMEVVNDL DYEAAEAAKE
SGLAFTRAAT AGTHSAFIAD LAGLILSQAA AARGEGGNLT SWPAPCVAGC CRRYPDAQDI
PAVSGGDVES VAAGADVVDA EPGGVDFVPS GSASAVDRPG PEAVELETPP SPYNPLTKET
PMSDHSSADS VIEGPRDDEV PAGSYTAPTD PRDTPVIPEE VNASSKWAMY SVFRVATALP
AEDDERRRLV EGSDEWAGQS GVDTRGWYDL SGLRANADLL VWWVSDDPAV LQDAYHRFRA
SGLGRHLEPV WSNVGVHRPA EFNKSHLPSC FAGIAPRRWA AFYPFIRSKE WYLLPAADRS
RMLREHGIVG AASSDVKAST LAAFALGDYE WILALEGDDL ARIVDVMKDL RYVEARRYVD
VDTPFFTGER VSPVVWADRQ MRA
