ID   CP137_MYCTO             Reviewed;         476 AA.
AC   P9WPM4; L0TDI2; O69653;
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 137;
DE            EC=1.14.-.-;
GN   Name=cyp137; OrderedLocusNames=MT3787;
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; AAK48154.1; -; Genomic_DNA.
DR   PIR; F70791; F70791.
DR   RefSeq; WP_003419754.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPM4; -.
DR   SMR; P9WPM4; -.
DR   EnsemblBacteria; AAK48154; AAK48154; MT3787.
DR   KEGG; mtc:MT3787; -.
DR   PATRIC; fig|83331.31.peg.4078; -.
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..476
FT                   /note="Putative cytochrome P450 137"
FT                   /id="PRO_0000426926"
FT   BINDING         422
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   476 AA;  52266 MW;  4FF0DBC89D8D0548 CRC64;
     MVLRSLASPA ALTDPKRCAS VVGVAAFAVR REHAPDALGG PPGLPAPRGF RAAFAAAYAV
     AYLAGGERRM LRLIRRYGPI MTMPILSLGD VAIVSDSALA KEVFTAPTDV LLGGEGVGPA
     AAIYGSGSMF VQEEPEHLRR RKLLTPPLHG AALDRYVPII ENSTRAAMHT WPVDRPFAML
     TVARSLMLDV IVKVIFGVDD PEEVRRLGRP FERLLNLGVS EQLTVRYALR RLGALRVWPA
     RARANTEIDD VVMALIAQRR ADPRLGERHD VLSLLVSARG ESGEQLSDSE IRDDLITLVL
     AGHETTATTL AWAFDLLLHH PDALRRVRAE AVGGGEAFTT AVINETLRVR PPAPLTARVA
     AQPLTIGGYR VEAGTRIVVH IIAINRSAEV YEHPHEFRPE RFLGTRPQTY AWVPFGGGVK
     RCLGANFSMR ELITVLHVLL REGEFTAVDD EPERIVRRSI MLVPRRGTRV RFRPAR