ID   CP143_MYCTO             Reviewed;         393 AA.
AC   P9WPL2; L0T7P2; O53936; P63723;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative cytochrome P450 143;
DE            EC=1.14.-.-;
GN   Name=cyp143; OrderedLocusNames=MT1834;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46104.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70929; C70929.
DR   RefSeq; WP_003408802.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPL2; -.
DR   SMR; P9WPL2; -.
DR   EnsemblBacteria; AAK46104; AAK46104; MT1834.
DR   KEGG; mtc:MT1834; -.
DR   PATRIC; fig|83331.31.peg.1975; -.
DR   HOGENOM; CLU_033716_0_1_11; -.
DR   Proteomes; UP000001020; 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_0000426932"
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