TAZG_ASPTN
ID TAZG_ASPTN Reviewed; 489 AA.
AC Q0CSA1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=FAD-linked oxidoreductase tazG {ECO:0000303|PubMed:35398258};
DE EC=1.-.-.- {ECO:0000305|PubMed:35398258};
DE AltName: Full=Azaphilone biosynthesis cluster protein G {ECO:0000303|PubMed:35398258};
DE Flags: Precursor;
GN Name=tazG {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03433;
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476597; EAU36707.1; -; Genomic_DNA.
DR RefSeq; XP_001212611.1; XM_001212611.1.
DR STRING; 33178.CADATEAP00010348; -.
DR EnsemblFungi; EAU36707; EAU36707; ATEG_03433.
DR GeneID; 4318028; -.
DR VEuPathDB; FungiDB:ATEG_03433; -.
DR eggNOG; ENOG502SJ3M; Eukaryota.
DR HOGENOM; CLU_018354_0_0_1; -.
DR OMA; GHGISDY; -.
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; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 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..489
FT /note="FAD-linked oxidoreductase tazG"
FT /id="PRO_5004170556"
FT DOMAIN 55..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 489 AA; 53694 MW; E93404DFAB44E12B CRC64;
MVAFSAILQT ALGLSAANDL TSLFGPYLSP QAEILYGNDT NFYAQLQQRW TDYKAPSYGA
GAIKPATAKD VQNVVKIANA NSIPFFVTGG GHGISDYHNF DGLSIDMGKF NTVERNAAGD
RLTIGGAVKI HQLTKPLAEW GKELPLGSCA CVGVVGATLG GGIGSLHGLR GLLVDYLEEV
EVVTASGDLI KASETEHKDL FWALRGAGSN YGIVTSATYR LPEVTNKGVY VNADYVYPVS
ANQSFFEVLE QFDNTLPPRL AITGASFFDR VNNKPVIAVN AVFFGPLEEA LPHLQPFESL
QPEMKNVSSI PAEQMMDAAF FSFFGMDNGA CTPNQHINIY TVALRQIHAP TFQSFYSKLV
DFWNANPTYQ GRLLIQRYSN EGPMAVPDDA TAYAYRDVKT YMNIEGFYAD SALDDAVNEF
ATLGRQEFVE TSGFDQLAVY SNYARGDEGP VAWYGERKLP KLSALKRKWD PEQRFSVNNP
VPLHWRTEL
