FC4_PHOAM
ID FC4_PHOAM Reviewed; 334 AA.
AC D7UTD0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Short-chain dehydrogenase/reductase {ECO:0000303|PubMed:21299202};
DE EC=1.1.1.- {ECO:0000269|PubMed:21299202, ECO:0000269|PubMed:22870285};
DE AltName: Full=Fusicoccin A biosynthetic gene clusters protein 4 {ECO:0000303|PubMed:22870285};
GN Name=fc-sdr {ECO:0000303|PubMed:21299202};
GN Synonyms=orf4 {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=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: Short-chain dehydrogenase/reductase; 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21299202,
CC ECO:0000269|PubMed:22870285}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB570429; BAJ10702.1; -; mRNA.
DR AlphaFoldDB; D7UTD0; -.
DR SMR; D7UTD0; -.
DR BioCyc; MetaCyc:MON-18712; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..334
FT /note="Short-chain dehydrogenase/reductase"
FT /id="PRO_0000445461"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 36..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 62..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 116..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 208..212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 240..242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 334 AA; 36689 MW; 9BEBC9C754AF08D4 CRC64;
MFGSFNSLKN AWAQVFPQAP DFTESSIPDL LGKVYIVTGA NSGLGKELSG ILYSKNAKVY
VAARSEAKAQ AAIEFIKAAH PHSKGDLVYL QIDLADLSAI KSSVNAFLSQ EARLDVLFNN
AGVLAPHDAP KTAQGYELNL GTNTIGTFLL TKLLLPTLLN TAKSSPKDSV RVIWVSSIAV
NFSEQGGLDM ENLDYHEDKS AVTKYAVSKV GNFLHSVELA RRHGANADGV VSVALNPGNL
DTELGRDRSW LETKILRTFV LYPPVFGAYT ELFAGLSDQI TAEMVRDNNW IGPWGRFCRI
REDIDQAARP RSEGGHGLAE RFWRWTEEQV KPYV
