ID   Q70AR5_STRPE            Unreviewed;       477 AA.
AC   Q70AR5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Putative cytochrome P450 {ECO:0000313|EMBL:CAE53716.1};
DE            EC=1.14.14.1 {ECO:0000313|EMBL:CAE53716.1};
GN   Name=cyp0913 {ECO:0000313|EMBL:CAE53716.1};
OS   Streptomyces peucetius.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1950 {ECO:0000313|EMBL:CAE53716.1};
RN   [1] {ECO:0000313|EMBL:CAE53716.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 27952 {ECO:0000313|EMBL:CAE53716.1};
RX   PubMed=15111132; DOI=10.1016/j.abb.2004.03.011;
RA   Parajuli N., Basnet D.B., Chan Lee H., Sohng J.K., Liou K.;
RT   "Genome analyses of Streptomyces peucetius ATCC 27952 for the
RT   identification and comparison of cytochrome P450 complement with other
RT   Streptomyces.";
RL   Arch. Biochem. Biophys. 425:233-241(2004).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; AJ605548; CAE53716.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70AR5; -.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd20620; CYP132-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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,
KW   ECO:0000313|EMBL:CAE53716.1}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  54129 MW;  547C9301ECE2AE5B CRC64;
     MCPPSSPTTY PSSPCDPPPL RKGLVRMTTT LVPPGPRGHP VLGSIREIQR DNVSAFMEAF
     RHHGDIVNFR GPLRINLLAH PDYVQHVLRD QHKRYPRPRK VQGCLSTIVG DGLVAAEGTS
     WLRSRRLTQP AFHRDILRRF GDSFTASTAE LLDGWERRAR DGEPLDIKSE MMHLSLANLA
     RALFRTEWTD EVSRIEPAVQ EALGFTHRRM TSPVDPLKFP SAARTRFRGA LETINSLLYP
     MVAERRRDGG GDDLVSLLID AVDPESGGMF TDEQIRDEVS GFFVAGHETV STALSWTWYL
     LSLNPESRRR LQAEVDEVLA GRVPTVDDLP KLTYTTMVLQ ESMRLYPPIF VYMRCAAEDD
     VIGGYHIPEG RWVVVCPYVT HRHPEFWDNP EGFEPERFTP ENSANRHRMA YLPFGAGPRK
     CIGDSFAMLQ MPLVVAMIAQ RFRLDLVEGQ QVFPEPAISL RPRDPLMMWL RPNEETP
//