BSC6_ALTBR
ID BSC6_ALTBR Reviewed; 397 AA.
AC C9K2Q2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=16-O-methyltransferase bsc6 {ECO:0000303|PubMed:19097780};
DE EC=2.1.1.- {ECO:0000269|PubMed:19097780};
DE AltName: Full=Brassicicene C biosynthetic gene cluster protein 6 {ECO:0000303|PubMed:19700326};
GN Name=bsc6 {ECO:0000303|PubMed:19097780};
GN Synonyms=orf6 {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, CATALYTIC ACTIVITY, COFACTOR, AND
RP PATHWAY.
RC STRAIN=ATCC 96836;
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 [2]
RP FUNCTION.
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 [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: 16-O-methyltransferase; 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=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000269|PubMed:19097780};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:19097780}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB465603; BAI44848.1; -; mRNA.
DR AlphaFoldDB; C9K2Q2; -.
DR SMR; C9K2Q2; -.
DR BioCyc; MetaCyc:MON-18717; -.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..397
FT /note="16-O-methyltransferase bsc6"
FT /id="PRO_0000445459"
FT ACT_SITE 302
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 397 AA; 44950 MW; 3B8440B0B7C40EAF CRC64;
MAVQETDLDK QLLQLSIQVA DLAARTDSRG SQKIQDFLIK TQQSLESPWE TLMRYYDLDF
QHVAIRIGCD MQVFTTLTTA DKPMKLQDIA NVNGASERLL GRVLRYLASI NTIEEVGKDT
FEANHITRTL SKPGIEGGIR LSSACQRPTN SALPDLLVER GFQDITSATE TAFNKAWASR
EPFFTWVRSQ PKIFEYLRLA LDVQFREDWL NAFPLESHLG DFASRADPEK VLFVDVGGNL
GIQCRGLKAK FPHLSGRIIL EDLQETIDVA LALEGVETLA QDYLTEQKVK GAKFYYYRNI
FHDNPDDRCR LILDALKPAM EESSLLLIDD KVLLNQGSHR HVTMLDLAMM AQVASHERTR
AQWQALLEGA GWKIEDIFQY SHEYDSIIVV KPAAQNA
