ANDJ_EMEVA
ID ANDJ_EMEVA Reviewed; 633 AA.
AC A0A097ZPG2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=FAD-binding monooxygenase andJ {ECO:0000303|PubMed:25216349};
DE EC=1.14.13.- {ECO:0000305|PubMed:25216349};
DE AltName: Full=Anditomin synthesis protein J {ECO:0000303|PubMed:25216349};
GN Name=andJ {ECO:0000303|PubMed:25216349};
OS Emericella variicolor (Aspergillus stellatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1549217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX PubMed=25216349; DOI=10.1021/ja508127q;
RA Matsuda Y., Wakimoto T., Mori T., Awakawa T., Abe I.;
RT "Complete biosynthetic pathway of anditomin: nature's sophisticated
RT synthetic route to a complex fungal meroterpenoid.";
RL J. Am. Chem. Soc. 136:15326-15336(2014).
CC -!- FUNCTION: FAD-binding monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of anditomin, a fungal meroterpenoid
CC (PubMed:25216349). The first step of the pathway is the synthesis of
CC 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM
CC (PubMed:25216349). DMOA is then converted to the phthalide compound
CC 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450
CC monooxygenase andK, which is further prenylated by the
CC prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349).
CC Further epoxidation by the FAD-dependent monooxygenase andE leads to
CC epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the
CC terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid
CC A through opening of the epoxide ring followed by the cyclization of
CC the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn
CC oxidized at the C-3 hydroxyl group to yield preandiloid B by the
CC dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely
CC responsible for the dehydrogenation of preandiloid B leading to the
CC enone preandiloid C, as well as for the intriguing structural
CC rearrangement to generate the bicyclo[2.2.2]octane core, transforming
CC preandiloid C into andiconin (PubMed:25216349). FAD-binding
CC monooxygenase andJ then produces andilesin D which is reduced by
CC dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of
CC acetyltransferase andG followed by a spontaneous acetate elimination
CC leads then to andilesin B, which is in turn substrate of the short
CC chain dehydrogenase andH to yield andilesin C (PubMed:25216349).
CC Finally, the dioxygenase andF catalyzes the transformation of andilesin
CC C to anditomin (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:H3JQW0};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:25216349}.
CC -!- DISRUPTION PHENOTYPE: Impairs the synthesis of anditomin but
CC accumulates andiconin (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AB981314; BAP81864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097ZPG2; -.
DR SMR; A0A097ZPG2; -.
DR BioCyc; MetaCyc:MON-19049; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; NADP; Oxidoreductase.
FT CHAIN 1..633
FT /note="FAD-binding monooxygenase andJ"
FT /id="PRO_0000436586"
FT BINDING 117..120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 127..129
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 129..130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 269..275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 292..293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT SITE 409
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
SQ SEQUENCE 633 AA; 70274 MW; ECEDC437A8176709 CRC64;
MAPAIQANSN GTMNVNGKCR DGHTAEQRNV MDDALPIEIT VEERGKAFAK DPWAHEYSVS
EQALRDQERL IDQYHHKVLI VGAGHGGLLF AVRLLQTGNF GINDILIVDE AAGFGGTWYW
NRYPGLMCDT ESYIYMPLLE ETGYMPREKY ASGPELRANA ERISHLWGLK RRALFRTAIK
ALDWNDAQGQ WKATAQGLGK LQQVKLSADF AIIATGLYAS PRIPDFPGLW NYKGPVFHPA
RWDYSVTGGT PERPEMTRLH NKRVAIVGTG ASAVQIVPQL ARHSKHLMVF QRTPSGVDQR
DNCYTDKARW KEIASTKGWQ RQRMENFNAF IGDPKSAPAV NMVGDRWTSM PSYSMTIGAN
GITKPGYQDE MREMDSIRQG KIRSRVHAIV HNPARADILS PNYPGWCKRP CFHDDYLAAF
NEPNVDLVDL QGKGSISFTA TGLAVADTQY EADVVIVSTG YTSPKDRSSP GSRANIAITG
RGGLEMERKW ESGLSTLHGV MTRDFPNLFF PGPAQSGVCT NQTYTLDQLA RHVAYIMARG
IQQCNGQAMV VEPSEEAERA WADQVVQRAG DSLTAFAACT STSLFSAAKM TKDQIMNAAR
LTTWREGIAS YVIELEAWRS EGTLQGLEIK RLA
