ID   CGOX_PROFF              Reviewed;         527 AA.
AC   O32434;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000250|UniProtKB:P32397};
DE            EC=1.3.3.15 {ECO:0000250|UniProtKB:P32397};
GN   Name=cgoX {ECO:0000250|UniProtKB:P32397}; Synonyms=hemY;
OS   Propionibacterium freudenreichii subsp. freudenreichii.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=66712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC
RC   10470 / NRRL B-3523;
RX   PubMed=9163953; DOI=10.1007/s002530050945;
RA   Hashimoto Y., Yamashita Y., Murooka Y.;
RT   "The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes
RT   enzymes and a regulator involved in the biosynthetic pathway from glutamate
RT   to protoheme.";
RL   Appl. Microbiol. Biotechnol. 47:385-392(1997).
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC       III. {ECO:0000250|UniProtKB:P32397}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2;
CC         Xref=Rhea:RHEA:43436, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57309, ChEBI:CHEBI:131725; EC=1.3.3.15;
CC         Evidence={ECO:0000250|UniProtKB:P32397};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC         Evidence={ECO:0000250|UniProtKB:P32397};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P32397};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P32397};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000250|UniProtKB:P32397}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32397}.
CC   -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC       oxidase family. Coproporphyrinogen III oxidase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D85417; BAA21909.1; -; Genomic_DNA.
DR   AlphaFoldDB; O32434; -.
DR   SMR; O32434; -.
DR   UniPathway; UPA00252; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Heme biosynthesis; Oxidoreductase.
FT   CHAIN           1..527
FT                   /note="Coproporphyrinogen III oxidase"
FT                   /id="PRO_0000135268"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33..38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         56..57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         64
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         78..81
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         300
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P56601"
FT   BINDING         448
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         487..489
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
SQ   SEQUENCE   527 AA;  55268 MW;  579CB0A3318BF938 CRC64;
     MSTTDRVTTP TPTVSGTDAP GPDASHCHLV VVGGGITGLA AAWQGMARGA RVSVVESDDH
     FGGKVVTDRR DGFLVEQGPD SFVAYRPAAL KLIEELGLSD QVIAPGGGRR VSLLSRGKLR
     PMPAGMGMVL PTRMWPFVTT TVLSWPDKIR AGLDLVIPRR LPDHDVAIGA FLRQRLGDGI
     VRRFADPMVG GIYGAGIDEL SLDAVLPSLR DNERDHRSLM VASLAGGRAS RRAARQRAAQ
     NNAQQNSSHQ NSTGQNNSAG TRGPAASPFR TLRGGLGQLI DALVDQLRAG GVELLVNTSV
     DLLGRDGVHL SDGRVLPADA VVLAGGVASS ARLLRPQLPA AARALAQIPL ASTTIVSLAW
     PVSAFDVAPD SQGWLEADAG PVSGLTASSI KFAGRAPDGS VLMRVFVPDK RGPLTDAPDD
     ELLSAVIDHV RPLLGVHGEP GLTQITRWHK VMPKYTVGHL ERAAVVDSTL AEQRPTWAVA
     GSALHGVGLP DCISDARHSA DEVIDAALAA TPSAPNRNAA TDRTETR