CGOX_MYCLE
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 03-AUG-2022, entry version 125.
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; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC 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; NP_301770.1; NC_002677.1.
DR RefSeq; WP_010908094.1; NC_002677.1.
DR AlphaFoldDB; Q50008; -.
DR SMR; Q50008; -.
DR STRING; 272631.ML1044; -.
DR EnsemblBacteria; CAC31425; CAC31425; CAC31425.
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 OMA; EHNQAVQ; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000000806; 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; -; 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;
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
