ID   BSC5_ALTBR              Reviewed;         523 AA.
AC   D1MX87;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Cytochrome P450 monooxygenase bsc5 {ECO:0000303|PubMed:19700326};
DE            EC=1.-.-.- {ECO:0000305|PubMed:19700326};
DE   AltName: Full=Brassicicene C biosynthetic gene cluster protein 5 {ECO:0000303|PubMed:19700326};
GN   Name=bsc5 {ECO:0000305}; Synonyms=orf5 {ECO:0000303|PubMed:19700326};
OS   Alternaria brassicicola (Dark leaf spot agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Brassicicola.
OX   NCBI_TaxID=29001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 96836;
RX   PubMed=19700326; DOI=10.1016/j.bmcl.2009.08.026;
RA   Hashimoto M., Higuchi Y., Takahashi S., Osada H., Sakaki T., Toyomasu T.,
RA   Sassa T., Kato N., Dairi T.;
RT   "Functional analyses of cytochrome P450 genes responsible for the early
RT   steps of brassicicene C biosynthesis.";
RL   Bioorg. Med. Chem. Lett. 19:5640-5643(2009).
RN   [2]
RP   FUNCTION.
RX   PubMed=19097780; DOI=10.1016/j.bmcl.2008.11.108;
RA   Minami A., Tajima N., Higuchi Y., Toyomasu T., Sassa T., Kato N., Dairi T.;
RT   "Identification and functional analysis of brassicicene C biosynthetic gene
RT   cluster in Alternaria brassicicola.";
RL   Bioorg. Med. Chem. Lett. 19:870-874(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=21299202; DOI=10.1021/ja107785u;
RA   Ono Y., Minami A., Noike M., Higuchi Y., Toyomasu T., Sassa T., Kato N.,
RA   Dairi T.;
RT   "Dioxygenases, key enzymes to determine the aglycon structures of
RT   fusicoccin and brassicicene, diterpene compounds produced by fungi.";
RL   J. Am. Chem. Soc. 133:2548-2555(2011).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the diterpene glucoside brassicicene C
CC       (PubMed:19097780). In the first step of the brassicicene C
CC       biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses
CC       both prenyl transferase and terpene cyclase activity, converts
CC       isopentenyl diphosphate and dimethylallyl diphosphate into
CC       geranylgeranyl diphosphate (GGDP) that is further converted into
CC       fusicocca-2,10(14)-diene, the first precursor for brassicicene C
CC       (PubMed:19097780). Fusicocca-2,10(14)-diene is then substrate of
CC       cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8
CC       position (PubMed:19700326). Oxidation at C-16 position to aldehyde is
CC       then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding
CC       fusicocca-2,10(14)-diene-8-beta,16-diol (PubMed:19700326). Follows the
CC       isomerization of the double bond and reduction of aldehyde to alcohol
CC       catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the
CC       diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The
CC       next step is the oxidation at the C-3 position of fusicocca-2,10(14)-
CC       diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent
CC       dioxygenase bsc9, to produce a triol compound (PubMed:21299202).
CC       Methylation of the hydroxy group at position 16 is performed by the
CC       methyltransferase bsc6 (PubMed:19097780). 16-O-methylation is followed
CC       by oxidation at the C-13 position to ketone and an alkyl shift of the
CC       methyl group leads to brassicicene C (Probable). Although the probable
CC       acetyltransferase bsc4 is included in the gene cluster, no acetylation
CC       reactions are necessary for brassicicene C biosynthesis. However, the
CC       fact that brassicicene E, which is a structurally related compound
CC       having an acetoxy group at position 12, was previously isolated from
CC       another strain of A.brassicicola suggests that the ATCC 96836 strain
CC       might also produce a small amount of brassicicene E (Probable).
CC       {ECO:0000269|PubMed:19097780, ECO:0000269|PubMed:19700326,
CC       ECO:0000269|PubMed:21299202, ECO:0000305|PubMed:19097780}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:19700326}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB506080; BAI52802.1; -; mRNA.
DR   AlphaFoldDB; D1MX87; -.
DR   SMR; D1MX87; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..523
FT                   /note="Cytochrome P450 monooxygenase bsc5"
FT                   /id="PRO_0000445453"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         459
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|UniProtKB:P04798"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   523 AA;  60169 MW;  FD26B83E366F401A CRC64;
     MLEGTLQDCW TSISKMQLHW TVLGLLPVLF IAILGPRVRQ IWVNYVHLTK IPSPHKKDYF
     CFVTETTRAE FLNECARLLR KGFASGDVIR LHASWDHIVV LSPSYAECLR ADEKFSPDTF
     SDKEMFGAVP GFEPYRFLCT HRDLVRNVIS MRLNRCFVPA TRYLSEAIDD ALRKQMGNDS
     EWREVPLGNA VLKILTQSSF RALQGPELCY DDEWLDIATQ YIVTSVTGVT ALRKLPKFLV
     PLIHWFHPDA IKSRRLLSRA RAKLIPFYEK RKKELYQARR NGTYRPEDAD AFGWYEELAD
     GRDYDPVVAQ LTVAVAATHS TTDFMCQFLS DMVRYPEYIQ PLRDELILAL KEKGWKASTI
     LQLPLLDSVM KESQRLKPVA MGFMRSIAQH DVYLQDAVKI PKNASVIVSA HSMRDATVYE
     NPDSFDGYRF INPTKHPESR HFTSVSVNHM GFGFGKHACP GRFFVNLETK ILIAHLLLKY
     DWKFANDGCP AIRTSGFDQV VDPSAKMLVR RRKEEIRIEA LYE