ID   CP143_MYCBO             Reviewed;         393 AA.
AC   P63724; A0A1R3XZB4; O53936; X2BIG2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative cytochrome P450 143;
DE            EC=1.14.-.-;
GN   Name=cyp143; OrderedLocusNames=BQ2027_MB1813C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00417.1; -; Genomic_DNA.
DR   RefSeq; NP_855466.1; NC_002945.3.
DR   RefSeq; WP_003408802.1; NC_002945.4.
DR   AlphaFoldDB; P63724; -.
DR   SMR; P63724; -.
DR   EnsemblBacteria; SIU00417; SIU00417; BQ2027_MB1813C.
DR   PATRIC; fig|233413.5.peg.1992; -.
DR   OMA; QPYFSPH; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..393
FT                   /note="Putative cytochrome P450 143"
FT                   /id="PRO_0000052305"
FT   BINDING         342
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  43541 MW;  8BCD1D50B471FAB8 CRC64;
     MTTPGEDHAG SFYLPRLEYS TLPMAVDRGV GWKTLRDAGP VVFMNGWYYL TRREDVLAAL
     RNPKVFSSRK ALQPPGNPLP VVPLAFDPPE HTRYRRILQP YFSPAALSKA LPSLRRHTVA
     MIDAIAGRGE CEAMADLANL FPFQLFLVLY GLPLEDRDRL IGWKDAVIAM SDRPHPTEAD
     VAAARELLEY LTAMVAERRR NPGPDVLSQV QIGEDPLSEI EVLGLSHLLI LAGLDTVTAA
     VGFSLLELAR RPQLRAMLRD NPKQIRVFIE EIVRLEPSAP VAPRVTTEPV TVGGMTLPAG
     SPVRLCMAAV NRDGSDAMST DELVMDGKVH RHWGFGGGPH RCLGSHLARL ELTLLVGEWL
     NQIPDFELAP DYAPEIRFPS KSFALKNLPL RWS