FC8_PHOAM
ID FC8_PHOAM Reviewed; 427 AA.
AC L0MXX3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=O-methyltransferase PaMT {ECO:0000303|PubMed:22870285};
DE EC=2.1.1.- {ECO:0000269|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 8 {ECO:0000303|PubMed:22870285};
GN Name=PaMT {ECO:0000303|PubMed:22870285};
GN Synonyms=orf8 {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, COFACTOR, 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-methyltransferase; 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 -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000269|PubMed:22870285};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for fusicoccin H {ECO:0000269|PubMed:22870285};
CC KM=563 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:22870285};
CC pH dependence:
CC Optimum pH is 9.0. {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 class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; AB686274; BAM71033.1; -; mRNA.
DR AlphaFoldDB; L0MXX3; -.
DR SMR; L0MXX3; -.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..427
FT /note="O-methyltransferase PaMT"
FT /id="PRO_0000445458"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 427 AA; 47679 MW; D76F148DE05006F0 CRC64;
MDDSKTNGRQ NASRIVALAN TIQKSVAELQ AVLDSKGLPA PSFAEDASPD PLPFEAQKAQ
DAVLDATAEL HDILLEPTAL VLKTISNEYV AFLGFISRYD IPNFVPLGGR VSFTDIAKKT
GFEEGIVKRL LRAAICRRIF QEPESGYVAH TKASKAMRSK ILLTFLRTGA DMGWYTIFKL
VDAAEKWPDV QEQDQTAFNL AHDVQGTYFE NVAKSAKNAE LFASGMATQW ELPGYELHHL
LDGYDWTGLG KAKVIDVGGF RGRISIALAE RFPDLDLLVQ DMEMNEADAH AAVPSALKDR
VHFMSRDIFT TQPVRADVYY IRQIFHDWSD KYCTKLLRAH TSQLEAGSSV LIHDCILPEV
PGSSLPLWKE RDMRAMDLGL VAHMNGRERS VDEWHKLVTE ADPRFKIRQI SQPEGSMLAL
IEVVFNA
