ID   CP143_MYCTU             Reviewed;         393 AA.
AC   P9WPL3; 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 37.
DE   RecName: Full=Putative cytochrome P450 143;
DE            EC=1.14.-.-;
GN   Name=cyp143; OrderedLocusNames=Rv1785c; ORFNames=MTV049.07c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44551.1; -; Genomic_DNA.
DR   PIR; C70929; C70929.
DR   RefSeq; NP_216301.1; NC_000962.3.
DR   RefSeq; WP_003408802.1; NZ_NVQJ01000037.1.
DR   AlphaFoldDB; P9WPL3; -.
DR   SMR; P9WPL3; -.
DR   STRING; 83332.Rv1785c; -.
DR   iPTMnet; P9WPL3; -.
DR   PaxDb; P9WPL3; -.
DR   DNASU; 885907; -.
DR   GeneID; 885907; -.
DR   KEGG; mtu:Rv1785c; -.
DR   TubercuList; Rv1785c; -.
DR   eggNOG; COG2124; Bacteria.
DR   OMA; QPYFSPH; -.
DR   PhylomeDB; P9WPL3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acetylation; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..393
FT                   /note="Putative cytochrome P450 143"
FT                   /id="PRO_0000052306"
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"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
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