BSC3_ALTBR
ID BSC3_ALTBR Reviewed; 274 AA.
AC E0D7H5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Short-chain dehydrogenase/reductase bsc3 {ECO:0000303|PubMed:19700326};
DE EC=1.-.-.- {ECO:0000305|PubMed:19097780};
DE AltName: Full=Brassicicene C biosynthetic gene cluster protein 3 {ECO:0000303|PubMed:19700326};
GN Name=bsc3 {ECO:0000305};
GN Synonyms=bc-sdr {ECO:0000303|PubMed:21299202},
GN orf3 {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], AND 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).
RN [2]
RP FUNCTION, AND PATHWAY.
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=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).
CC -!- FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of the diterpene glucoside brassicicene
CC C (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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:19097780}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB570249; BAJ15868.1; -; mRNA.
DR AlphaFoldDB; E0D7H5; -.
DR SMR; E0D7H5; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..274
FT /note="Short-chain dehydrogenase/reductase bsc3"
FT /id="PRO_0000445462"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 29..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 55..56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 100..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 173..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 274 AA; 28830 MW; A487A837416B8839 CRC64;
MSQSTLVIIG AGGIGEAIAR RVGPGKEVLL GDWSNALLQE ATQRMKRDGF RVTSQHVNIS
SHDSVIQFAE KAQSLGQVMH VVISAGLSPV SSTRETILAV NLAGTGFCIA EFGKLIGHGG
TCVVISSLAG YTLAQDVPHG VIQHLARTSP SDVLGLPLLR ETVLDQWSAY GVSKRVNYVQ
VQDASLSWAR RGARINSISP GAIQTPMLSL ESQASKEEVV HDLAQNVPCK RVGDSGEVAH
VAAFLLGSES SFVTGTDILV DGGALAYLSR DTSS
