FC11_PHOAM
ID FC11_PHOAM Reviewed; 453 AA.
AC H7CE84;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=O-glucose prenyltransferase PaPT {ECO:0000303|PubMed:22870285};
DE EC=2.5.1.- {ECO:0000269|PubMed:22287087};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 11 {ECO:0000303|PubMed:22870285};
GN Name=PaPT {ECO:0000303|PubMed:22870285};
GN Synonyms=orf11 {ECO:0000303|PubMed:22870285};
OS Phomopsis amygdali (Fusicoccum amygdali).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214568;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RX PubMed=22870285; DOI=10.1371/journal.pone.0042090;
RA Noike M., Ono Y., Araki Y., Tanio R., Higuchi Y., Nitta H., Hamano Y.,
RA Toyomasu T., Sassa T., Kato N., Dairi T.;
RT "Molecular breeding of a fungus producing a precursor diterpene suitable
RT for semi-synthesis by dissection of the biosynthetic machinery.";
RL PLoS ONE 7:E42090-E42090(2012).
RN [2]
RP FUNCTION.
RX PubMed=17360612; DOI=10.1073/pnas.0608426104;
RA Toyomasu T., Tsukahara M., Kaneko A., Niida R., Mitsuhashi W., Dairi T.,
RA Kato N., Sassa T.;
RT "Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3084-3088(2007).
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=22287087; DOI=10.1002/cbic.201100725;
RA Noike M., Liu C., Ono Y., Hamano Y., Toyomasu T., Sassa T., Kato N.,
RA Dairi T.;
RT "An enzyme catalyzing O-prenylation of the glucose moiety of fusicoccin A,
RT a diterpene glucoside produced by the fungus Phomopsis amygdali.";
RL ChemBioChem 13:566-573(2012).
CC -!- FUNCTION: O-glucose prenyltransferase; part of the 2 gene clusters that
CC mediate the biosynthesis of fusicoccins, diterpene glucosides that
CC display phytohormone-like activity and function as potent activators of
CC plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and
CC cause the plant disease constriction canker (PubMed:22870285,
CC PubMed:22287087). The first step in the pathway is performed by the
CC fusicoccadiene synthase PaFS that possesses both prenyl transferase and
CC terpene cyclase activity, converting isopentenyl diphosphate and
CC dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and
CC successively converting GGDP into fusicocca-2,10(14)-diene, a precursor
CC for fusicoccin H (PubMed:17360612). The second step is the oxidation at
CC the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield
CC fusicocca-2,10(14)-diene-8-beta-ol (PubMed:22870285). The cytochrome
CC P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-
CC 16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol
CC (PubMed:22870285). The dioxygenase fc-dox then catalyzes the 16-
CC oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an
CC aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al)
CC (PubMed:21299202, PubMed:22870285). The short-chain
CC dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde
CC to yield fusicocca-1,10(14)-diene-8-beta,16-diol (PubMed:21299202,
CC PubMed:22870285). The next step is the hydroxylation at C-9 performed
CC by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin
CC H aglycon which is glycosylated to fusicoccin H by the O-
CC glycosyltransferase PaGT (PubMed:22870285). Hydroxylation at C-12 by
CC the cytochrome P450 monooxygenase PaP450-4 leads then to the production
CC of fusicoccin Q and is followed by methylation by the O-
CC methyltransferase PaMT to yield fusicoccin P (PubMed:22870285).
CC Fusicoccin P is further converted to fusicoccin J via prenylation by
CC the O-glucose prenyltransferase PaPT (PubMed:22287087). Cytochrome P450
CC monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield
CC dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin
CC A by the O-acetyltransferase PaAT-2 (PubMed:22870285). Finally, a
CC another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin
CC A (PubMed:22870285). {ECO:0000269|PubMed:17360612,
CC ECO:0000269|PubMed:21299202, ECO:0000269|PubMed:22287087,
CC ECO:0000269|PubMed:22870285}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.490 uM for fusicoccin P {ECO:0000269|PubMed:22287087};
CC KM=32.6 uM for fusicoccin H {ECO:0000269|PubMed:22287087};
CC KM=8.3 uM for dimethylallyl diphosphate (with fusicoccin P)
CC {ECO:0000269|PubMed:22287087};
CC KM=35.96 uM for dimethylallyl diphosphate (with fusicoccin H)
CC {ECO:0000269|PubMed:22287087};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:22287087};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:22287087};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22287087,
CC ECO:0000269|PubMed:22870285}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB669436; BAL68129.1; -; mRNA.
DR AlphaFoldDB; H7CE84; -.
DR SMR; H7CE84; -.
DR BioCyc; MetaCyc:MON-18714; -.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..453
FT /note="O-glucose prenyltransferase PaPT"
FT /id="PRO_0000445463"
FT BINDING 95..96
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 453 AA; 50745 MW; 11301F80F1EDC766 CRC64;
MANVVLDGSA APAKAGLPLD LSSPSKQTNF PTELESNSNA DFWWRLCRPE MAGLFKQAGG
YTELQQESHL RFVREHCAPW MGTVPTGHMA NEAVAPVEMS VNYISSRDEG VLRFQMEPFT
AVSGPHTQAD DPSGKKAVCS MLRSFQHALG DVDLTWTWQL VDKFMVTAPD EVARLREAER
TSLPPPLDLY QRTPQFNFAF DLSPDKKSMK TYFLPLAKSL VTGSSALDYC LDAVRSLEPH
GEGLSPVADL LHQFFNTSCP GHMSCDYLGI DSTNPKRSRV KLYVSSQQHN SFNFIRAVFT
LGGIAKDEAT LRGLEFLRSI WHLLVNVDEG ELPDSSDRPA KQLPFFLGCL YFSFEWRAGD
RLPLVKLYVP QWQYAQSDRK IAKNISASLR KLGRDEAADE YLTHIKQTFP RADLDGNVSI
HNQVSYAYSA ETGAYLTIYY SVNSKAVARD QIY
