FC6_PHOAM
ID FC6_PHOAM Reviewed; 406 AA.
AC L0MZK0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=O-glycosyltransferase PaGT {ECO:0000303|PubMed:22870285};
DE EC=2.4.1.- {ECO:0000269|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 6 {ECO:0000303|PubMed:22870285};
GN Name=PaGT {ECO:0000303|PubMed:22870285};
GN Synonyms=orf6 {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, CATALYTIC ACTIVITY, 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.
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-glycosyltransferase; 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). The
CC first step in the pathway is performed by the fusicoccadiene synthase
CC PaFS that possesses both prenyl transferase and terpene cyclase
CC activity, converting isopentenyl diphosphate and dimethylallyl
CC diphosphate into geranylgeranyl diphosphate (GGDP) and successively
CC converting GGDP into fusicocca-2,10(14)-diene, a precursor for
CC fusicoccin H (PubMed:17360612). The second step is the oxidation at the
CC 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=44 uM for dideacetyl-fusicoccin A {ECO:0000269|PubMed:22870285};
CC KM=520 uM for UDP-glucose {ECO:0000269|PubMed:22870285};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:22870285};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:22870285};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22870285}.
CC -!- SIMILARITY: Belongs to the afumC glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB686272; BAM71031.1; -; mRNA.
DR AlphaFoldDB; L0MZK0; -.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR008441; AfumC-like_glycosyl_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF05704; Caps_synth; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..406
FT /note="O-glycosyltransferase PaGT"
FT /id="PRO_0000445465"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 46575 MW; 9C4F33E9F83F8EF4 CRC64;
MSPPSQIKPP QGTTPVPPSE LDPRSDEEIV RSISAHVKPT DSEKNMWAYW HSGWENMPPW
TKRNVVHWAR MLGTEWTVRV LDGIPGSANY YERFVPPHLL PSAMRERRMS GPYVATHSAD
FVRLPLLFLY GGCWLDVGAI LVRSIQDVWD VLADPKQSYE FAAFTYMMRP GEASIINTWM
MGRKNMELLR RWHDTFLHLW GDKSSCDGLH KHPLLSHLRP LSSLTHGLIT DENNEPVAKT
DKIIDYGAQV YCLDRLRDLV DTNDGWNGRQ CIEEKTFLLA ALDEMWYYQP KTDYLGSRQF
ELLTTRYDAP EPQRGDAEEF VNDMLANTML MKFCHGLKDA MVSSLADIWD DPKHDGTDCA
PGTFAEYLRW GTLHLRQTRT LEPVKLTAPA GKLHHVAMFE PFPSTN
