ID   TAZL_ASPTN              Reviewed;         493 AA.
AC   Q0CS92;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=FAD-linked oxidoreductase tazL {ECO:0000303|PubMed:35398258};
DE            EC=1.-.-.- {ECO:0000305|PubMed:35398258};
DE   AltName: Full=Azaphilone biosynthesis cluster protein L {ECO:0000303|PubMed:35398258};
DE   Flags: Precursor;
GN   Name=tazL {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03442;
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-linked oxidoreductase; 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   -!- 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 oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; CH476597; EAU36716.1; -; Genomic_DNA.
DR   RefSeq; XP_001212620.1; XM_001212620.1.
DR   STRING; 33178.CADATEAP00010358; -.
DR   EnsemblFungi; EAU36716; EAU36716; ATEG_03442.
DR   GeneID; 4317486; -.
DR   VEuPathDB; FungiDB:ATEG_03442; -.
DR   eggNOG; ENOG502SJ3M; Eukaryota.
DR   HOGENOM; CLU_018354_0_0_1; -.
DR   OMA; ITSATYE; -.
DR   OrthoDB; 350817at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..493
FT                   /note="FAD-linked oxidoreductase tazL"
FT                   /id="PRO_5004170553"
FT   DOMAIN          63..235
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   493 AA;  53081 MW;  2FB49585B485A445 CRC64;
     MRSNTVILAA LPLVASAAST SGNWGGGVNY SKIFGGGLSA NASIHYPGQP DYNTTTVQRW
     STWAEPTFAV TIKPATDEDV QYIIRTANKY NLTFLATGGG HGGETGFATV KHAVNIDLSN
     FKENVLDLEA NTLTVGPGNS FSAFETNLYN AGKMVPVGNA FCVNMIGATI GAGVGPYQGL
     HGLVIDALRS VRLVTASGDI VTASDEENPD LFWAVRGAGA NFGIITSATY EIFDAPNNGN
     VVLAEFAYPG SVNGSLWQLL ESWGETYPKE MGLTMSASYS QTTGTTSSSA SLTYFGTQEA
     AQPWIDQLLA LNPTQWRNAT LPWSEVSQNS GFGTGASVCA TGKYNNHPSV GAKQTSVSTY
     IEVFNQYVEI MKARPWLTSA LVVQRFNTTA TLAVPESKRG VYPGRDFSSL IILENYYDGP
     RHDADVYRFS KKLRSQLVAT SGFDSLQTYI NYAHGDEGPE VWYGKDNLPR LVQLKRQWDP
     EGKFGPGNPI PLA