BSC2_ALTBR
ID BSC2_ALTBR Reviewed; 525 AA.
AC D1MX86;
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 bsc2 {ECO:0000303|PubMed:19700326};
DE EC=1.-.-.- {ECO:0000305|PubMed:19700326};
DE AltName: Full=Brassicicene C biosynthetic gene cluster protein 2 {ECO:0000303|PubMed:19700326};
GN Name=bsc2 {ECO:0000305}; Synonyms=orf2 {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; AB506079; BAI52801.1; -; mRNA.
DR AlphaFoldDB; D1MX86; -.
DR SMR; D1MX86; -.
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..525
FT /note="Cytochrome P450 monooxygenase bsc2"
FT /id="PRO_0000445452"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 456
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 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 525 AA; 59843 MW; B4A337640AE20077 CRC64;
MESAQIHSTR DSLFILWLTT LLVSVLATAA YIKFQSRPRP YSGFPLVTLG GPSETDSSHA
ANWFRRGRAL VNKGLSELSG AFQISNGSGY WIILPSKYMD ELRNHPDMSL RDALREENFP
NYRGFDGFRQ AFKDSTFTQE VIRVKVTQSL GLITANLANE CQHALQENLG ESREWQQRFI
IEDILNIVAQ LTSRVFLGER LCRDKEWLQI TKEYARNSFM GSEELRQCLP LTRPLMQFFM
PACTQLRKFS AAARRLIDPE VQARKRRAEE AIKLGKKPPK VEDTIGWMVE VARGRQVDYV
GGQLALSIAA IHSSTDNLSK AVVKLCEMPE IVAPLREEIT TVLESTDGWS KPALYRMKLL
DSFLKEVQRL APFTIVGMHR RVMKGYVLSD GTHLPKNSRI MVMNDKLRDS SVYEDPDTFK
YDRFARLREQ PGQEDQHQLA STSSEFATFG HGEHACPGRF FAANQLKIIM ACLLLKYDFC
FQPGQAEKAR VIPFEMVETI DPTLKIEVRR RSEELDVTKV AKETA
