ID   CP126_MYCBO             Reviewed;         414 AA.
AC   P63712; A0A1R3XWF1; P77903; X2BG53;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative cytochrome P450 126;
DE            EC=1.14.-.-;
GN   Name=cyp126; OrderedLocusNames=BQ2027_MB0801;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT99400.1; -; Genomic_DNA.
DR   RefSeq; NP_854459.1; NC_002945.3.
DR   RefSeq; WP_003898584.1; NC_002945.4.
DR   AlphaFoldDB; P63712; -.
DR   SMR; P63712; -.
DR   EnsemblBacteria; SIT99400; SIT99400; BQ2027_MB0801.
DR   PATRIC; fig|233413.5.peg.871; -.
DR   OMA; ESERHWL; -.
DR   Proteomes; UP000001419; 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_0000052281"
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