ID   CP132_MYCTO             Reviewed;         461 AA.
AC   P9WPN2; L0T9I0; P77900;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Putative cytochrome P450 132;
DE            EC=1.14.-.-;
GN   Name=cyp132; OrderedLocusNames=MT1439;
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}.
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DR   EMBL; AE000516; AAK45704.1; -; Genomic_DNA.
DR   PIR; H70899; H70899.
DR   RefSeq; WP_003407260.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPN2; -.
DR   SMR; P9WPN2; -.
DR   EnsemblBacteria; AAK45704; AAK45704; MT1439.
DR   KEGG; mtc:MT1439; -.
DR   PATRIC; fig|83331.31.peg.1545; -.
DR   HOGENOM; CLU_001570_5_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; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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..461
FT                   /note="Putative cytochrome P450 132"
FT                   /id="PRO_0000426922"
FT   BINDING         409
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   461 AA;  52186 MW;  EA176E6EAEA05791 CRC64;
     MATATTQRPL KGPAKRMSTW TMTREAITIG FDAGDGFLGR LRGSDITRFR CAGRRFVSIS
     HPDYVDHVLH EARLKYVKSD EYGPIRATAG LNLLTDEGDS WARHRGALNS TFARRHLRGL
     VGLMIDPIAD VTAALVPGAQ FDMHQSMVET TLRVVANALF SQDFGPLVQS MHDLATRGLR
     RAEKLERLGL WGLMPRTVYD TLIWCIYSGV HLPPPLREMQ EITLTLDRAI NSVIDRRLAE
     PTNSADLLNV LLSADGGIWP RQRVRDEALT FMLAGHETTA NAMSWFWYLM ALNPQARDHM
     LTELDDVLGM RRPTADDLGK LAWTTACLQE SQRYFSSVWI IAREAVDDDI IDGHRIRRGT
     TVVIPIHHIH HDPRWWPDPD RFDPGRFLRC PTDRPRCAYL PFGGGRRICI GQSFALMEMV
     LMAAIMSQHF TFDLAPGYHV ELEATLTLRP KHGVHVIGRR R