FC9_PHOAM
ID FC9_PHOAM Reviewed; 497 AA.
AC L0MXJ3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=O-acetyltransferase PaAT-1 {ECO:0000303|PubMed:22870285};
DE EC=2.3.1.- {ECO:0000269|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 9 {ECO:0000303|PubMed:22870285};
GN Name=PaAT-1 {ECO:0000303|PubMed:22870285};
GN Synonyms=orf9 {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-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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22870285}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR EMBL; AB686275; BAM71034.1; -; mRNA.
DR AlphaFoldDB; L0MXJ3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glycoprotein; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..497
FT /note="O-acetyltransferase PaAT-1"
FT /id="PRO_0000445460"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 497 AA; 56707 MW; 970894BC4A002C73 CRC64;
MIELGQSYST IQAMTKQKPL KSLRQRVKEN QTPPNRSQNH LGILRPSFSQ HSRERKMLHS
TSWLDGLRGI SATCVVVHHC TLQWFGWHIH EPWFPGQSFL KLPVIRLLIS GSPHVYIFFV
ISGYSLSYKP LKLSRQGRFD EAASVLSSSI FRRHARLFVP TTIVTFFCAI MTQLNWYGKA
EHMPGVAVPA WEPPHLDNIW AQLNNFAWNE LLFMDPVGRT VAKGDPGEQV KQLHNPYDYV
LWTLPVEFNS SMVLLMFLMA FSRVESRARM AFCLAMAVLF QCFFIYWALF LFFSGMLICD
LRLELGEALS TRAPSKDTRS WSKHLFVRAI GVGCFVLSLC ALSTPHLAFG GREAPGFVTL
ASMIPERFGD QLLMPIAAIG LVLTLDHHPF LQVLFTNSFA QYMGRISFAL FLVHGPLLNT
LGHALGRRFI ALIGGDTEER YLVAISLTAM VFWLMTILLA DFVYQYVDLA SVQVSKWAYQ
RLLRTEEQPG KYEWKSR
