FC2_PHOAM
ID FC2_PHOAM Reviewed; 399 AA.
AC E0D7H6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase fc-dox {ECO:0000303|PubMed:21299202};
DE EC=1.14.11.- {ECO:0000269|PubMed:21299202, ECO:0000269|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 2 {ECO:0000303|PubMed:22870285};
GN Name=fc-dox {ECO:0000303|PubMed:21299202};
GN Synonyms=orf2 {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, AND PATHWAY.
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 [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=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).
RN [4]
RP 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).
CC -!- FUNCTION: Alpha-ketoglutarate-dependent dioxygenase; part of the 2 gene
CC clusters that mediate the biosynthesis of fusicoccins, diterpene
CC glucosides that display phytohormone-like activity and function as
CC potent activators of plasma membrane H(+)-ATPases in plants by
CC modifying 14-3-3 proteins and cause the plant disease constriction
CC canker (PubMed:21299202, PubMed:22870285). The first step in the
CC pathway is performed by the fusicoccadiene synthase PaFS that possesses
CC both prenyl transferase and terpene cyclase activity, converting
CC 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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P37610};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21299202,
CC ECO:0000269|PubMed:22870285}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; AB570428; BAJ15869.1; -; mRNA.
DR AlphaFoldDB; E0D7H6; -.
DR BioCyc; MetaCyc:MON-18711; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..399
FT /note="Alpha-ketoglutarate-dependent dioxygenase fc-dox"
FT /id="PRO_0000445457"
FT REGION 371..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 203
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 355
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 367
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
SQ SEQUENCE 399 AA; 46007 MW; 47049993E0C6DC1A CRC64;
MGSTAEDFVI KPMKGEHGFG AEIYGLDVNN ITDEQVDRLR DTIQRYLLVV LKHQHDETPQ
KNWELLNRLS PDAPKFTPEE WALMYNPDPQ GAGILPKLGY LVLPGTERLF LMGKGYQGED
HWGLKDIDIP EVFADAYYSK PLPHEDYHNG VARFQSWHID GPSYKIDHPM FTSFRIIKFP
EGEQTVDWAD GSGLTKKVKA GRTAFFSSAK LYDMLTKEEQ AIADYSWAEY MYFPYEWILR
CRGNPQGLLV ACEGREVPDE QMDAMPRNPE DQLVLPLVWV NPVTGGKHFH VQPNIVRRVF
VRSGPDEEPK IIDDVKEVRD FFTKFQYRII RPENIYVGPE EEGDQLLFFN WGVMHSKIDY
PIEMGTRTTH QGWLAGDRPP KGPVPIPDPR ARSSIYYQK
