ID   CP136_MYCTO             Reviewed;         492 AA.
AC   P9WPM6; L0TEE3; P95099;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Putative cytochrome P450 136;
DE            EC=1.14.-.-;
GN   Name=cyp136; OrderedLocusNames=MT3145;
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; AAK47477.1; -; Genomic_DNA.
DR   PIR; D70649; D70649.
DR   RefSeq; WP_003899900.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPM6; -.
DR   SMR; P9WPM6; -.
DR   EnsemblBacteria; AAK47477; AAK47477; MT3145.
DR   KEGG; mtc:MT3145; -.
DR   PATRIC; fig|83331.31.peg.3388; -.
DR   HOGENOM; CLU_001570_15_0_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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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..492
FT                   /note="Putative cytochrome P450 136"
FT                   /id="PRO_0000426925"
FT   BINDING         439
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   492 AA;  56228 MW;  B0A78FCE95622F3D CRC64;
     MATIHPPAYL LDQAKRRFTP SFNNFPGMSL VEHMLLNTKF PEKKLAEPPP GSGLKPVVGD
     AGLPILGHMI EMLRGGPDYL MFLYKTKGPV VFGDSAVLPG VAALGPDAAQ VIYSNRNKDY
     SQQGWVPVIG PFFHRGLMLL DFEEHMFHRR IMQEAFVRSR LAGYLEQMDR VVSRVVADDW
     VVNDARFLVY PAMKALTLDI ASMVFMGHEP GTDHELVTKV NKAFTITTRA GNAVIRTSVP
     PFTWWRGLRA RELLENYFTA RVKERREASG NDLLTVLCQT EDDDGNRFSD ADIVNHMIFL
     MMAAHDTSTS TATTMAYQLA AHPEWQQRCR DESDRHGDGP LDIESLEQLE SLDLVMNESI
     RLVTPVQWAM RQTVRDTELL GYYLPKGTNV IAYPGMNHRL PEIWTDPLTF DPERFTEPRN
     EHKRHRYAFT PFGGGVHKCI GMVFDQLEIK TILHRLLRRY RLELSRPDYQ PRWDYSAMPI
     PMDGMPIVLR PR