ID   C135B_MYCTO             Reviewed;         472 AA.
AC   P9WPM8; L0T464; O53765; P63715;
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 135B1;
DE            EC=1.14.-.-;
GN   Name=cyp135B1; OrderedLocusNames=MT0594;
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; AAK44817.1; -; Genomic_DNA.
DR   PIR; G70932; G70932.
DR   RefSeq; WP_003402992.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPM8; -.
DR   SMR; P9WPM8; -.
DR   EnsemblBacteria; AAK44817; AAK44817; MT0594.
DR   KEGG; mtc:MT0594; -.
DR   PATRIC; fig|83331.31.peg.626; -.
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..472
FT                   /note="Putative cytochrome P450 135B1"
FT                   /id="PRO_0000426924"
FT   REGION          442..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         388
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   472 AA;  50688 MW;  B7E2898BEE80863F CRC64;
     MSGTSSMGLP PGPRLSGSVQ AVLMLRHGLR FLTACQRRYG SVFTLHVAGF GHMVYLSDPA
     AIKTVFAGNP SVFHAGEANS MLAGLLGDSS LLLIDDDVHR DRRRLMSPPF HRDAVARQAG
     PIAEIAAANI AGWPMAKAFA VAPKMSEITL EVILRTVIGA SDPVRLAALR KVMPRLLNVG
     PWATLALANP SLLNNRLWSR LRRRIEEADA LLYAEIADRR ADPDLAARTD TLAMLVRAAD
     EDGRTMTERE LRDQLITLLV AGHDTTATGL SWALERLTRH PVTLAKAVQA ADASAAGDPA
     GDEYLDAVAK ETLRIRPVVY DVGRVLTEAV EVAGYRLPAG VMVVPAIGLV HASAQLYPDP
     ERFDPDRMVG ATLSPTTWLP FGGGNRRCLG ATFAMVEMRV VLREILRRVE LSTTTTSGER
     PKLKHVIMVP HRGARIRVRA TRDVSATSQA TAQGAGCPAA RGGGPSRAVG SQ