ID   C1AZD5_RHOOB            Unreviewed;       398 AA.
AC   C1AZD5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:BAH50063.1};
GN   OrderedLocusNames=ROP_18160 {ECO:0000313|EMBL:BAH50063.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50063.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH50063.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH50063.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; AP011115; BAH50063.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1AZD5; -.
DR   STRING; 632772.ROP_18160; -.
DR   KEGG; rop:ROP_18160; -.
DR   PATRIC; fig|632772.20.peg.1904; -.
DR   HOGENOM; CLU_033716_0_2_11; -.
DR   Proteomes; UP000002212; 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   CDD; cd11035; P450cam-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR46696:SF2; CYTOCHROME P450 130; 1.
DR   PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ   SEQUENCE   398 AA;  44365 MW;  8BF341EBEAB8E531 CRC64;
     MDFDVYDQTL AMPEDVFQER AAELRAIGPV VYSTAHGGHW IVTRYEEIHQ VLRDPETFSS
     YPNNLVNAGQ GKFIPIELDP PEHTFYRQAL QPLFSPKRMK ELEPQIRDVI NELIDAFVAR
     GETEFISEFA HELPTRVFLA LMGWPLEDAE MFTKTTDVAL QGIPGGTEEE SAKAREDAAN
     QIFGYFGAIV AGVRSGENTS DSLTAQIINT PIEMEDGVRL LTDEELYRMF FLLLIAGLHT
     VQGSLAWGII HLANNPGQRQ EIVDDPDTIP AAVEEILRIE AAVIAGRRAT REVELGGVTI
     AQGDQLIVLL CSANRDGGEF EDPDELRIDR SPNRHLSFGA GPHRCIGSHL ARIELKLAME
     AIHRRLPDYR LVPEDPPILH ATQVRGCIRL PITFTPSS
//