ID   CP140_MYCTO             Reviewed;         438 AA.
AC   P9WPL8; L0T9I7; O08464; P63721;
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 140;
DE            EC=1.14.-.-;
GN   Name=cyp140; OrderedLocusNames=MT1929;
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=AAK46201.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46201.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70515; E70515.
DR   RefSeq; WP_003409406.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPL8; -.
DR   SMR; P9WPL8; -.
DR   EnsemblBacteria; AAK46201; AAK46201; MT1929.
DR   GeneID; 45425853; -.
DR   KEGG; mtc:MT1929; -.
DR   PATRIC; fig|83331.31.peg.2076; -.
DR   HOGENOM; CLU_033716_2_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; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
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..438
FT                   /note="Putative cytochrome P450 140"
FT                   /id="PRO_0000426929"
FT   BINDING         381
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   438 AA;  48872 MW;  0463B3EECF358744 CRC64;
     MKDKLHWLAM HGVIRGIAAI GIRRGDLQAR LIADPAVATD PVPFYDEVRS HGALVRNRAN
     YLTVDHRLAH DLLRSDDFRV VSFGENLPPP LRWLERRTRG DQLHPLREPS LLAVEPPDHT
     RYRKTVSAVF TSRAVSALRD LVEQTAINLL DRFAEQPGIV DVVGRYCSQL PIVVISEILG
     VPEHDRPRVL EFGELAAPSL DIGIPWRQYL RVQQGIRGFD CWLEGHLQQL RHAPGDDLMS
     QLIQIAESGD NETQLDETEL RAIAGLVLVA GFETTVNLLG NGIRMLLDTP EHLATLRQHP
     ELWPNTVEEI LRLDSPVQLT ARVACRDVEV AGVRIKRGEV VVIYLAAANR DPAVFPDPHR
     FDIERPNAGR HLAFSTGRHF CLGAALARAE GEVGLRTFFD RFPDVRAAGA GSRRDTRVLR
     GWSTLPVTLG PARSMVSP