ID   CP123_MYCTO             Reviewed;         402 AA.
AC   P9WPP4; L0T7F5; P63707; P77902;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative cytochrome P450 123;
DE            EC=1.14.-.-;
GN   Name=cyp123; OrderedLocusNames=MT0790;
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; AAK45032.1; -; Genomic_DNA.
DR   PIR; A70707; A70707.
DR   RefSeq; WP_003403911.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPP4; -.
DR   SMR; P9WPP4; -.
DR   EnsemblBacteria; AAK45032; AAK45032; MT0790.
DR   KEGG; mtc:MT0790; -.
DR   PATRIC; fig|83331.31.peg.849; -.
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..402
FT                   /note="Putative cytochrome P450 123"
FT                   /id="PRO_0000426916"
FT   BINDING         350
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   402 AA;  45421 MW;  76AD843019361798 CRC64;
     MTVRVGDPEL VLDPYDYDFH EDPYPYYRRL RDEAPLYRNE ERNFWAVSRH HDVLQGFRDS
     TALSNAYGVS LDPSSRTSEA YRVMSMLAMD DPAHLRMRTL VSKGFTPRRI RELEPQVLEL
     ARIHLDSALQ TESFDFVAEF AGKLPMDVIS ELIGVPDTDR ARIRALADAV LHREDGVADV
     PPPAMAASIE LMRYYADLIA EFRRRPANNL TSALLAAELD GDRLSDQEIM AFLFLMVIAG
     NETTTKLLAN AVYWAAHHPG QLARVFADHS RIPMWVEETL RYDTSSQILA RTVAHDLTLY
     DTTIPEGEVL LLLPGSANRD DRVFDDPDDY RIGREIGCKL VSFGSGAHFC LGAHLARMEA
     RVALGALLRR IRNYEVDDDN VVRVHSSNVR GFAHLPISVQ AR