FC10_PHOAM
ID FC10_PHOAM Reviewed; 518 AA.
AC L0N065;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Fusicoccin H C-9 hydroxylase {ECO:0000303|PubMed:22870285};
DE EC=1.-.-.- {ECO:0000269|PubMed:22870285};
DE AltName: Full=Cytochrome P450 monooxygenase PaP450-4 {ECO:0000303|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 10 {ECO:0000303|PubMed:22870285};
GN Name=PaP450-4 {ECO:0000303|PubMed:22870285};
GN Synonyms=orf10 {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, DISRUPTION
RP 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: Cytochrome P450 monooxygenase; part of the 2 gene clusters
CC that 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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22870285}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Accumulates fusicoccin H.
CC {ECO:0000269|PubMed:22870285}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB686276; BAM71035.1; -; mRNA.
DR AlphaFoldDB; L0N065; -.
DR SMR; L0N065; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Fusicoccin H C-9 hydroxylase"
FT /id="PRO_0000445449"
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 456
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 518 AA; 59208 MW; 32C508403ED67999 CRC64;
MAKFTVTSLE RHLLLISTVI AVLAALIVSR GCNYLLKRWK LSAYPLYEDK KVTPIEELHS
SRDLIAKGFA KSQGKEIWRI NTTIGEVLVV SPKYIEKFRY GHGCSAAAYT ERELPISAPG
YEPFTFASNE WRQRNADIIL HRLTGLVSNR KIELSEELSN ALESRWTNST DWHAVSLFQT
MTAIVAQTTQ YFFTNRELCR NDAYIQSLFA YSSLAFTEGR SLMKWPRVLH PLVARFHPAS
QNLQSALENV NKHIFPFVRE RRAEISRRRF EAAQSGKETP LADEWVAWLD EKAGNEDYNP
GVAMVSFSVA SFHTTTDFMC QLLCDLARNP AIIEQLKEEA SDVLRDHTWT KSSFARLDLM
DRCMKESQRL KPIGAVFLKS RAQKDISVEN GNIIPAGSLF VVSGHWMHDP AIYPEPEKFD
PGRHLRHAEE SKPNKPKQFT AVSPEHMGWG YGKHSCPGRF FAATVAKMLL THILFKYEFK
LPDGKLNQHA YEFTTEILVR RRIEEGALNL DSFDSIDR
