ID   CGOX_MYCLE              Reviewed;         451 AA.
AC   Q50008;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-SEP-2026, entry version 139.
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;
GN   OrderedLocusNames=ML1044;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; U15181; AAA62958.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31425.1; -; Genomic_DNA.
DR   PIR; F87039; F87039.
DR   RefSeq; WP_010908094.1; NC_002677.1.
DR   AlphaFoldDB; Q50008; -.
DR   SMR; Q50008; -.
DR   STRING; 272631.gene:17574870; -.
DR   KEGG; mle:ML1044; -.
DR   PATRIC; fig|272631.5.peg.1876; -.
DR   Leproma; ML1044; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_1_11; -.
DR   OrthoDB; 4496419at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004729; F:protoporphyrinogen oxidase activity, oxygen as acceptor; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 1.
DR   Gene3D; 3.90.660.20; Protoporphyrinogen oxidase, mitochondrial, domain 2; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR   InterPro; IPR050464; Zeta_carotene_desat/Oxidored.
DR   NCBIfam; NF008841; PRK11883.1-1; 1.
DR   NCBIfam; TIGR00562; proto_IX_ox; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Heme biosynthesis; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..451
FT                   /note="Coproporphyrinogen III oxidase"
FT                   /id="PRO_0000135264"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         36..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         58..61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         242
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P56601"
FT   BINDING         393
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         429..431
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
SQ   SEQUENCE   451 AA;  46580 MW;  DF76EE1655CA2056 CRC64;
     MTSRSYCVVG GGISGLTAAY RLRVATGDDV AITLFDPGDR LGGVLRTECV GGQPMDLGAE
     AFLLRRPEVP ALLAELGLSE RQRATTDARP LIYSQQRLHS LPPDTVAGIP SSATSVAGLV
     DDATVARIGA EAVRPLSWEP GSDPAMAELV ADRFGEQAVA RLVDPLLGGV YAGSAATIGL
     RAGAPSVAAA LDCGATSLME AVRQGLPPVA AGPVFGALDG GYQVLIDELV RRSRLQWVAA
     TVVGLDRGTC GWTLVDDTGA CWSADGVILA VPAPRLVRLL QQIAPRTVAA ASRIVSASSA
     VVALSVPRDT TFPQNSGVLV ASGERLRAKA VTLSSRKWGL QGDTQLVRLS FGKFGDQVAS
     TASDDELLAW AVSDLAAVFD VTVDPVDVCV QRWIDAMPQY GPGHADLVAE VRAGLPPTLV
     VAGSHMDGIG VPACISAAGR AIEALQAEVA R
//