ID   CP139_MYCTO             Reviewed;         430 AA.
AC   P9WPM0; D0EW72; F2GKM3; O86330; P63719;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Putative cytochrome P450 139;
DE            EC=1.14.-.-;
GN   Name=cyp139; OrderedLocusNames=MT1706;
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=AAK45973.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45973.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70985; D70985.
DR   RefSeq; WP_003901231.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPM0; -.
DR   SMR; P9WPM0; -.
DR   EnsemblBacteria; AAK45973; AAK45973; MT1706.
DR   GeneID; 45425635; -.
DR   KEGG; mtc:MT1706; -.
DR   PATRIC; fig|83331.31.peg.1831; -.
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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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..430
FT                   /note="Putative cytochrome P450 139"
FT                   /id="PRO_0000426928"
FT   BINDING         372
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   430 AA;  47865 MW;  DCBA4CF08FAD1A94 CRC64;
     MRYPLGEALL ALYRWRGPLI NAGVGGHGYT YLLGAEANRF VFANADAFSW SQTFESLVPV
     DGPTALIVSD GADHRRRRSV VAPGLRHHHV QRYVATMVSN IDTVIDGWQP GQRLDIYQEL
     RSAVRRSTAE SLFGQRLAVH SDFLGEQLQP LLDLTRRPPQ VMRLQQRVNS PGWRRAMAAR
     KRIDDLIDAQ IADARTAPRP DDHMLTTLIS GCSEEGTTLS DNEIRDSIVS LITAGYETTS
     GALAWAIYAL LTVPGTWESA ASEVARVLGG RVPAADDLSA LTYLNGVVHE TLRLYSPGVI
     SARRVLRDLW FDGHRIRAGR LLIFSAYVTH RLPEIWPEPT EFRPLRWDPN AADYRKPAPH
     EFIPFSGGLH RCIGAVMATT EMTVILARLV ARAMLQLPAQ RTHRIRAANF AALRPWPGLT
     VEIRKSAPAQ