ID   TAZF_ASPTN              Reviewed;         561 AA.
AC   Q0CSA3;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=FAD-binding monooxygenase tazF {ECO:0000303|PubMed:35398258};
DE            EC=1.14.13.- {ECO:0000305|PubMed:35398258};
DE   AltName: Full=Azaphilone biosynthesis cluster protein F {ECO:0000303|PubMed:35398258};
GN   Name=tazF {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03431;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=35398258; DOI=10.1016/j.fgb.2022.103694;
RA   Sun W.W., Li C.Y., Chiang Y.M., Lin T.S., Warren S., Chang F.R.,
RA   Wang C.C.C.;
RT   "Characterization of a silent azaphilone biosynthesis gene cluster in
RT   Aspergillus terreus NIH 2624.";
RL   Fungal Genet. Biol. 160:103694-103694(2022).
CC   -!- FUNCTION: FAD-binding monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of azaterrilone A and other azaphilones, a
CC       class of fungal metabolites characterized by a highly oxygenated
CC       pyrano-quinone bicyclic core and exhibiting a broad range of
CC       bioactivities (PubMed:35398258). The first step of the pathway begins
CC       with the non-reducing polyketide synthase tazA that assembles one
CC       acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series
CC       of Claisen condensations, methylation, PT-mediated cyclization, and
CC       finally releases the first hexaketide precursor through the R-domain.
CC       The tazA product then undergoes reduction on its terminal ketone and
CC       the following pyran-ring formation by yet undetermined enzyme(s).
CC       Dehydration and enoyl reduction, possibly involving the trans-enoyl
CC       reductase tazE leads to the next intermediate. TazD is predicted as an
CC       acetyltransferase and might catalyze the acetylation steps leading to
CC       the synthesis of azaterrilone A. Azaterrilone A is not the final
CC       product of the taz pathway and both the highly reducing polyketide
CC       synthase tazB and the dual enzyme tazHJ catalyze late steps of the
CC       pathway, leading to the production of the 2 final stereoisomers that
CC       contain additional polyketide modification whose structures have still
CC       to be determined (Probable). {ECO:0000269|PubMed:35398258,
CC       ECO:0000305|PubMed:35398258}.
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.
CC       {ECO:0000305|PubMed:35398258}.
CC   -!- INDUCTION: Expression is positively regulated by the azaterrilone A
CC       cluster-specific transcription factor tazR.
CC       {ECO:0000269|PubMed:35398258}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CH476597; EAU36705.1; -; Genomic_DNA.
DR   RefSeq; XP_001212609.1; XM_001212609.1.
DR   EnsemblFungi; EAU36705; EAU36705; ATEG_03431.
DR   GeneID; 4317823; -.
DR   VEuPathDB; FungiDB:ATEG_03431; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006937_6_2_1; -.
DR   OMA; PFRCKRV; -.
DR   OrthoDB; 405736at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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   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; 3.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..561
FT                   /note="FAD-binding monooxygenase tazF"
FT                   /id="PRO_0000456066"
FT   BINDING         74..77
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         84..86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         86..87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         92
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         212..218
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         235..236
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   SITE            334
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
SQ   SEQUENCE   561 AA;  63906 MW;  E73FAE7D2403A9F2 CRC64;
     MPSNESTCLG SDRNMQTAWK LNASTPGFTP KKLRVVCIGA GLSGLTLAYK LKHERPMDFV
     DLRIYEKNHE VGGTWLDNVY PGVGCDIPSP SYVFPFEPNP DWSKFYVGGA EIQQYILRTT
     AKYGLKERIV FNTRLLKAEW NEDSAKWKLQ LEQDGRVFDD ETDVLINGTG CLSQWKWPDI
     EGLDCFKGKL LHSARWDPEY NWEGKRIAVI GNGSSALQLV PSLQPKAAKL VNYIRHPTWV
     SVNFCPDLTR DGMGSNFEFT EEEKQQFRDD PEMFFQYRKK VEHGVNTVLQ MMISGSGEHK
     FLHETVEGLM RQRLADRPDL IDKMIPNYEI GCRRLSPGDG YLEALQAANA RPSFANINRI
     TPTGFETDEG EEEFDLIACA TGFNTSYIPP FKMTGRGGRR LDVEWKDKPA AYFATCAAGF
     PNYFIFAGPN APIGHGSVNR MIWFQADYML NWVEKIATED IRSVAVKDSA VRDFNEFAKE
     NLKRFVWSKG CHAWYSKKTD GEDNIVTAMY PGSLLHFKVY LDKIRGEHFD IQYNTSNMFG
     FLGNGELALE REKDGDMAFY M