ID   CP126_MYCTO             Reviewed;         414 AA.
AC   P9WPN8; L0T4P8; P63711; P77903;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Putative cytochrome P450 126;
DE            EC=1.14.-.-;
GN   Name=cyp126; OrderedLocusNames=MT0802;
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; AAK45044.1; -; Genomic_DNA.
DR   PIR; E70708; E70708.
DR   RefSeq; WP_003898584.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPN8; -.
DR   SMR; P9WPN8; -.
DR   EnsemblBacteria; AAK45044; AAK45044; MT0802.
DR   KEGG; mtc:MT0802; -.
DR   PATRIC; fig|83331.31.peg.861; -.
DR   HOGENOM; CLU_033716_0_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   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..414
FT                   /note="Putative cytochrome P450 126"
FT                   /id="PRO_0000426919"
FT   BINDING         363
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   414 AA;  45954 MW;  2CCCBE0250818E3F CRC64;
     MTTAAGLSGI DLTDLDNFAD GFPHHLFAIH RREAPVYWHR PTEHTPDGEG FWSVATYAET
     LEVLRDPVTY SSVTGGQRRF GGTVLQDLPV AGQVLNMMDD PRHTRIRRLV SSGLTPRMIR
     RVEDDLRRRA RGLLDGVEPG APFDFVVEIA AELPMQMICI LLGVPETDRH WLFEAVEPGF
     DFRGSRRATM PRLNVEDAGS RLYTYALELI AGKRAEPADD MLSVVANATI DDPDAPALSD
     AELYLFFHLL FSAGAETTRN SIAGGLLALA ENPDQLQTLR SDFELLPTAI EEIVRWTSPS
     PSKRRTASRA VSLGGQPIEA GQKVVVWEGS ANRDPSVFDR ADEFDITRKP NPHLGFGQGV
     HYCLGANLAR LELRVLFEEL LSRFGSVRVV EPAEWTRSNR HTGIRHLVVE LRGG