ID   CP136_MYCTU             Reviewed;         492 AA.
AC   P9WPM7; L0TEE3; P95099;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Putative cytochrome P450 136;
DE            EC=1.14.-.-;
GN   Name=cyp136; OrderedLocusNames=Rv3059; ORFNames=MTCY22D7.22c;
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 ALA-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; CCP45868.1; -; Genomic_DNA.
DR   PIR; D70649; D70649.
DR   RefSeq; NP_217575.1; NC_000962.3.
DR   RefSeq; WP_003899900.1; NZ_NVQJ01000011.1.
DR   AlphaFoldDB; P9WPM7; -.
DR   SMR; P9WPM7; -.
DR   STRING; 83332.Rv3059; -.
DR   iPTMnet; P9WPM7; -.
DR   PaxDb; P9WPM7; -.
DR   DNASU; 888883; -.
DR   GeneID; 888883; -.
DR   KEGG; mtu:Rv3059; -.
DR   TubercuList; Rv3059; -.
DR   eggNOG; COG2124; Bacteria.
DR   OMA; AHMCLGL; -.
DR   PhylomeDB; P9WPM7; -.
DR   Proteomes; UP000001584; 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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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   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..492
FT                   /note="Putative cytochrome P450 136"
FT                   /id="PRO_0000052295"
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"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
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