BSC9_ALTBR
ID BSC9_ALTBR Reviewed; 398 AA.
AC D7UTD1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase bsc9 {ECO:0000303|PubMed:21299202};
DE EC=1.14.11.- {ECO:0000269|PubMed:21299202};
DE AltName: Full=Brassicicene C biosynthetic gene cluster protein 9 {ECO:0000303|PubMed:19700326};
DE AltName: Full=Brassicicene-dioxygenase {ECO:0000303|PubMed:21299202};
GN Name=bsc7 {ECO:0000305};
GN Synonyms=bc-dox {ECO:0000303|PubMed:21299202},
GN orf7 {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,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=96836;
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.
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: Alpha-ketoglutarate dependent dioxygenase; part of the gene
CC cluster that mediates the biosynthesis of the diterpene glucoside
CC brassicicene C (PubMed:21299202). In the first step of the brassicicene
CC C biosynthesis, the bifunctionnal diterpene synthase bsc8 that
CC possesses both prenyl transferase and terpene cyclase activity,
CC converts 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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P37610};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21299202}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase 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; AB570430; BAJ10703.1; -; mRNA.
DR AlphaFoldDB; D7UTD1; -.
DR BioCyc; MetaCyc:MON-18715; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..398
FT /note="Alpha-ketoglutarate-dependent dioxygenase bsc9"
FT /id="PRO_0000445456"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 212
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 365
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 377
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
SQ SEQUENCE 398 AA; 45701 MW; 8DD7C1F889D0B5C5 CRC64;
MASTSSTSTD GHLNIRPMVH GSDKKLNFGA YITGLDLNNA SDAEVDQLRE AILRHKIVVI
KGQQAEKPDK NWEMIKKLDP MHHMITQEEF GQLFHPTGEG LIAMLKLATV PTTEHGHIHL
MGKGYQGDDH YGLKKLNLGE AFAGNYYSKP LAEEDFRAGV TRFQSWHMDG PLYKVHPPYI
SSLRFIQLPD GEQTVEWADG SGLSLKTKPG RTAFFSTSQL YDMLTDEERA MVDNSAVEYM
YYPYEWIRGC RGNPNGLNVA DEGREKPLDA MEEIARDERW TKTYPMVWFN ELTKEKSLQV
QPNCVRRLLI RRSADQKEPE IIEGPERVRE FMNKLQQRIV RPEYVYVGPE EEGDHVFWYN
WGMMHSKIDY PIAYGPRIVH QGWIPSHRVP RGPTAVAH
