CP132_MYCBO
ID CP132_MYCBO Reviewed; 461 AA.
AC P59954; A0A1R3XY81; X2BHI2;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative cytochrome P450 132;
DE EC=1.14.-.-;
GN Name=cyp132; OrderedLocusNames=BQ2027_MB1429C;
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; SIU00032.1; -; Genomic_DNA.
DR RefSeq; NP_855081.1; NC_002945.3.
DR RefSeq; WP_003407260.1; NC_002945.4.
DR AlphaFoldDB; P59954; -.
DR SMR; P59954; -.
DR EnsemblBacteria; SIU00032; SIU00032; BQ2027_MB1429C.
DR PATRIC; fig|233413.5.peg.1564; -.
DR OMA; IFRRMKM; -.
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; 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..461
FT /note="Putative cytochrome P450 132"
FT /id="PRO_0000052286"
FT BINDING 409
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 461 AA; 52186 MW; EA176E6EAEA05791 CRC64;
MATATTQRPL KGPAKRMSTW TMTREAITIG FDAGDGFLGR LRGSDITRFR CAGRRFVSIS
HPDYVDHVLH EARLKYVKSD EYGPIRATAG LNLLTDEGDS WARHRGALNS TFARRHLRGL
VGLMIDPIAD VTAALVPGAQ FDMHQSMVET TLRVVANALF SQDFGPLVQS MHDLATRGLR
RAEKLERLGL WGLMPRTVYD TLIWCIYSGV HLPPPLREMQ EITLTLDRAI NSVIDRRLAE
PTNSADLLNV LLSADGGIWP RQRVRDEALT FMLAGHETTA NAMSWFWYLM ALNPQARDHM
LTELDDVLGM RRPTADDLGK LAWTTACLQE SQRYFSSVWI IAREAVDDDI IDGHRIRRGT
TVVIPIHHIH HDPRWWPDPD RFDPGRFLRC PTDRPRCAYL PFGGGRRICI GQSFALMEMV
LMAAIMSQHF TFDLAPGYHV ELEATLTLRP KHGVHVIGRR R