ID   CGOX_MYCTO              Reviewed;         452 AA.
AC   P9WMP0; L0TAB5; O53230; P0A5A7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=MT2751;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47066.1; -; Genomic_DNA.
DR   RefSeq; WP_003413871.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMP0; -.
DR   SMR; P9WMP0; -.
DR   KEGG; mtc:MT2751; -.
DR   PATRIC; fig|83331.31.peg.2962; -.
DR   HOGENOM; CLU_009629_3_1_11; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000001020; Chromosome.
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; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
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..452
FT                   /note="Coproporphyrinogen III oxidase"
FT                   /id="PRO_0000427270"
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         390
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
FT   BINDING         426..428
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P32397"
SQ   SEQUENCE   452 AA;  46846 MW;  6DFA1F57BEE2810F CRC64;
     MTPRSYCVVG GGISGLTSAY RLRQAVGDDA TITLFEPADR LGGVLRTEHI GGQPMDLGAE
     AFVLRRPEMP ALLAELGLSD RQLASTGARP LIYSQQRLHP LPPQTVVGIP SSAGSMAGLV
     DDATLARIDA EAARPFTWQV GSDPAVADLV ADRFGDQVVA RSVDPLLSGV YAGSAATIGL
     RAAAPSVAAA LDRGATSVTD AVRQALPPGS GGPVFGALDG GYQVLLDGLV RRSRVHWVRA
     RVVQLERGWV LRDETGGRWQ ADAVILAVPA PRLARLVDGI APRTHAAARQ IVSASSAVVA
     LAVPGGTAFP HCSGVLVAGD ESPHAKAITL SSRKWGQRGD VALLRLSFGR FGDEPALTAS
     DDQLLAWAAD DLVTVFGVAV DPVDVRVRRW IEAMPQYGPG HADVVAELRA GLPPTLAVAG
     SYLDGIGVPA CVGAAGRAVT SVIEALDAQV AR
//