BSC8_ALTBR
ID BSC8_ALTBR Reviewed; 697 AA.
AC C9K2Q3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Fusicoccadiene synthase {ECO:0000303|PubMed:19097780};
DE Short=FS {ECO:0000303|PubMed:19097780};
DE Includes:
DE RecName: Full=Fusicocca-2,10(14)-diene synthase {ECO:0000303|PubMed:19097780};
DE EC=4.2.3.43 {ECO:0000269|PubMed:19097780};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:19097780};
DE Short=GGDP synthase {ECO:0000303|PubMed:19097780};
DE Short=GGS {ECO:0000303|PubMed:19097780};
DE EC=2.5.1.29 {ECO:0000269|PubMed:19097780};
GN Name=bsc8 {ECO:0000303|PubMed:19097780};
GN Synonyms=orf8 {ECO:0000303|PubMed:19097780};
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, AND 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: Multifunctional diterpene synthase; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate = diphosphate + fusicocca-2,10(14)-
CC diene; Xref=Rhea:RHEA:26245, ChEBI:CHEBI:33019, ChEBI:CHEBI:52463,
CC ChEBI:CHEBI:57533; EC=4.2.3.43;
CC Evidence={ECO:0000269|PubMed:19097780};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:19097780};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:19097780}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase
CC family. {ECO:0000305}.
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DR EMBL; AB465604; BAI44849.1; -; mRNA.
DR AlphaFoldDB; C9K2Q3; -.
DR SMR; C9K2Q3; -.
DR PRIDE; C9K2Q3; -.
DR BioCyc; MetaCyc:MON-18716; -.
DR BRENDA; 4.2.3.43; 9662.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 2.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1..697
FT /note="Fusicoccadiene synthase"
FT /id="PRO_0000418512"
FT REGION 1..330
FT /note="Fusicocca-2,10(14)-diene synthase"
FT /evidence="ECO:0000305|PubMed:19097780"
FT REGION 184..187
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 232..236
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 321..322
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 331..697
FT /note="Geranylgeranyl diphosphate synthase"
FT /evidence="ECO:0000305|PubMed:19097780"
FT REGION 351..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 416
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 419
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 448
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 464
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 465
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 542
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 543
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 580
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 587
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 597
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 697 AA; 78573 MW; 56D9954136F432B2 CRC64;
MKYQFSIIVD PATYDNEGLS NGIDLRKNNF THLEDRGAIR AQQDWATHIA PIKQFKGTLG
HDYSFMTVCV PECIPIRLEI ISYANEFAFM YDDDTELDTE NNTSAENDKL MGTFLAGTQG
WSPPQDQSSS GKTRILKQLF SEMMEIDKEC AIATMKAWAE FLRVGSSRQH GTVFTRLKDY
LPYRIKDVGE MFWFGVVTFG MALHIPDHEM DACHKLMEPA WIAVGLANDV FSWPKERDAS
QRLGRTHVVN AVWVVMQEHG FSQEQARQYC RELAAQFVAQ YLDNIRNIKN EESISPDLRT
YVEAMQYSIS GNVIWSKFCP RYNPEKRFNQ TQLDWMQNGL PSTVELDGAS NTSSSFLSTS
THGSPASGSQ TTIESKDGWT ADSSGIVSLL LNCSLPPLSH KVISAPLTYV DSLPSKGTRD
MFLDALNHWL HVDEQRASQV KMAIRMLHNA SLMLDDVQDG SRLRRSKPSA HRVFGVAQTT
NSAAFLVNES IKLIRELAGD QGVAAVLEKL TSLFVGQAQD LHSSRNLSPP SLTEYIQTID
QKTSALFELA SRLMCLCSTA TVVPNSSLSR FCILLGRFFQ IRDDYQNLTS PEYTKQKGFC
DDLDSGTYTL PLVYAISQQS ENFLLQNLLS TRLAEGTLDD DQKRLALDQM QLVKTNEFLR
KILDSLYDEL RAELQCISSS FASENPQMEL MLMMLKL
