FC13_PHOAM
ID FC13_PHOAM Reviewed; 490 AA.
AC L0MZK4;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=O-acetyltransferase PaAT-2 {ECO:0000303|PubMed:22870285};
DE EC=2.3.1.- {ECO:0000269|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 12 {ECO:0000303|PubMed:22870285};
GN Name=PaAT-2 {ECO:0000303|PubMed:22870285};
GN Synonyms=orf13 {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,
RP BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, 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-acetyltransferase; part of the 2 gene clusters that mediate
CC the biosynthesis of fusicoccins, diterpene glucosides that display
CC phytohormone-like activity and function as potent activators of plasma
CC membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause
CC the plant disease constriction canker (PubMed:22870285). The first step
CC in the pathway is performed by the fusicoccadiene synthase PaFS that
CC possesses both prenyl transferase and terpene cyclase activity,
CC converting isopentenyl diphosphate and dimethylallyl diphosphate into
CC geranylgeranyl diphosphate (GGDP) and successively converting GGDP into
CC fusicocca-2,10(14)-diene, a precursor for fusicoccin H
CC (PubMed:17360612). The second step is the oxidation at the C-8 position
CC by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-
CC 2,10(14)-diene-8-beta-ol (PubMed:22870285). The cytochrome P450
CC monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16
CC 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=170 uM for dideacetyl-fusicoccin A {ECO:0000269|PubMed:22870285};
CC KM=63 uM for acetyl-CoA {ECO:0000269|PubMed:22870285};
CC pH dependence:
CC Optimum pH is 8.5. {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 -!- DISRUPTION PHENOTYPE: Accumulates fusicoccin J.
CC {ECO:0000269|PubMed:22870285}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AB686277; BAM71036.1; -; mRNA.
DR AlphaFoldDB; L0MZK4; -.
DR SMR; L0MZK4; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Transferase.
FT CHAIN 1..490
FT /note="O-acetyltransferase PaAT-2"
FT /id="PRO_0000445464"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 490 AA; 55134 MW; 5240321DBE723623 CRC64;
MSQTTVPVDR IVPFHRFDDA IGLRNSILVW TLRFDDVLDA AKLRDSLNAL LSIGNWKRLG
GRVRKKRDGK LEVHIPESFT PQHPAADFSH TKLDCCIDEH ALGRRLPVAT EKPKLYESST
IFHEFATREN PPLTIEDYCN SDLPQIGLHV VSFTDATLVS VSWPHTMSDA VGIQTLLINW
SRVMAGREIE VQHLEDVESN PLDNLEAGEG GTLKQEEWIL KSSLVTGVWF VIWVIRYIWT
IIWVSQESKL IYLPARTIKA LRREAEDSLV EQTQTLVPGH LEKPFVSDGD VITAWAVRMA
CLHQASQQTS QQSITIINAL DVRARLPDLF KQNTAYVGNF AFALFTKTTV GQVMSTSLGE
LAHTVRRSLL EQVPQAQIRA MFQELRKTRM GALIVGTATS SPLIFSNWSK TKICEVVDFS
PAVIRPGKQG PVISEPGKPV YHHSLHTKRS QTARDAFNIL GKDPAGNYWI AAWLPPCAWP
RIKEEMQKLP
