ANDE_EMEVA
ID ANDE_EMEVA Reviewed; 471 AA.
AC A0A097ZPF7;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=FAD-dependent monooxygenase andE {ECO:0000303|PubMed:25216349};
DE EC=1.-.-.- {ECO:0000269|PubMed:25216349};
DE AltName: Full=Anditomin synthesis protein E {ECO:0000303|PubMed:25216349};
GN Name=andE {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, AND CATALYTIC ACTIVITY.
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-dependent 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; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:25216349}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AB981314; BAP81859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097ZPF7; -.
DR SMR; A0A097ZPF7; -.
DR BioCyc; MetaCyc:MON-19044; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..471
FT /note="FAD-dependent monooxygenase andE"
FT /id="PRO_0000436581"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 318..322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 471 AA; 53256 MW; A8B741FCB0796813 CRC64;
MEQQSLKVVI VGGSIAGLTL AHCLHRANID HVVLEKRAEI APQEGASIGI WPNGARMLEQ
LGLYGELEKL TEPLNLMHIA FPDGFSFEDL LPTTINQRFG YPIIFLDRQK FLETLYRKYP
DKSKIVTNTR VAEVQSSEKC ARVITEDGTM YEGDIVVGAD GVHSLVRREM WKLGDSKQPG
SVPSREKTGM TVEYSCVYGI SSPIVGLRAG ESVNSYMDGM TVLTFHGKGG RVYWFLIQKL
HQKYTYPNTP RYTVEDAERL CTDHRDTTIW KDIRIGHLWD NREVVSMTAL EENLFAKWHF
HRIGLMGDSI HKMTPNIGQG ANSAIEDAAV FSSLLVHMMT SEGPGRPSSA RIQRLLHDYQ
ACRYERAEMI YHRSRFGARF QSRDDAVKLI VGRYVVPRIR NRLANISSML IANGEIIQYL
PFPKRSGPGW EKFRNKGEWM PYTPFALFSA ILLVQHVVPL LGLTSPLLLA S
