ID   TAZP_ASPTN              Reviewed;         403 AA.
AC   Q0CS93;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=FAD-dependent monooxygenase tazP {ECO:0000303|PubMed:35398258};
DE            EC=1.-.-.- {ECO:0000305|PubMed:35398258};
DE   AltName: Full=Azaphilone biosynthesis cluster protein P {ECO:0000303|PubMed:35398258};
GN   Name=tazP {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03441;
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-dependent 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:A6T923};
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 paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CH476597; EAU36715.1; -; Genomic_DNA.
DR   RefSeq; XP_001212619.1; XM_001212619.1.
DR   STRING; 33178.CADATEAP00010357; -.
DR   EnsemblFungi; EAU36715; EAU36715; ATEG_03441.
DR   GeneID; 4317485; -.
DR   VEuPathDB; FungiDB:ATEG_03441; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_3_2_1; -.
DR   OMA; SLTIHWA; -.
DR   OrthoDB; 1248412at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..403
FT                   /note="FAD-dependent monooxygenase tazP"
FT                   /id="PRO_0000456073"
FT   BINDING         64..65
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         350..354
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         354
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   403 AA;  44669 MW;  8A6D552D27C8A5FF CRC64;
     MSILKLVKGV LYGEGEHHEK PKKTHIVIIG AGLTGLLLAQ GLRKLNARLE AEGQSAPFTF
     SIHERDESSF YRGGGFSLTI HWALQQLYDI LPEELSARIF ECVGNPDAIK NGQMGSFTFL
     NLRTGEPALK TTIPPGWKGA RMSRVRFLQL LMTDLDIHYS HRLSQITFPT DNTVRAHFEN
     GDQETGNLLI GADGANSVVR RFVYGAENSK NTQLPIRMLN CRSEYPLEEL EACLRVDPHL
     FHAGDPVQDG YFMFAFLDMP PAGSKNGKAG VQLTISWPYE SGYLGQEAPS DPPTELPEQL
     AWLKHMAKHW ANPVHDLIYG MPDDSIVRVI RVQEWMPNDA NRRPTDGRIT TVGDAAHLMT
     SFRGENANHG VVDVAKLLAL LAPSGNKPTD LREVPVPVST DDA