TAZE_ASPTN
ID TAZE_ASPTN Reviewed; 303 AA.
AC Q0CS94;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Trans-enoyl reductase tazE {ECO:0000303|PubMed:35398258};
DE EC=1.-.-.- {ECO:0000305|PubMed:35398258};
DE AltName: Full=Azaphilone biosynthesis cluster protein E {ECO:0000303|PubMed:35398258};
GN Name=tazE {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03440;
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: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of azaterrilone A and other azaphilones, a class of
CC fungal metabolites characterized by a highly oxygenated pyrano-quinone
CC bicyclic core and exhibiting a broad range of bioactivities
CC (PubMed:35398258). The first step of the pathway begins with the non-
CC reducing polyketide synthase tazA that assembles one acetyl-CoA starter
CC unit, five malonyl-CoA units, and catalyzes a series of Claisen
CC condensations, methylation, PT-mediated cyclization, and finally
CC releases the first hexaketide precursor through the R-domain. The tazA
CC product then undergoes reduction on its terminal ketone and the
CC 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 zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CH476597; EAU36714.1; -; Genomic_DNA.
DR RefSeq; XP_001212618.1; XM_001212618.1.
DR STRING; 33178.CADATEAP00010356; -.
DR EnsemblFungi; EAU36714; EAU36714; ATEG_03440.
DR GeneID; 4317484; -.
DR VEuPathDB; FungiDB:ATEG_03440; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_5_1; -.
DR OMA; PDHGAFQ; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..303
FT /note="Trans-enoyl reductase tazE"
FT /id="PRO_0000456072"
FT BINDING 44..49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 136..143
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 170..173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 193..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 211
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 246..247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 265..269
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 303 AA; 32019 MW; F0568DB8884E3CA3 CRC64;
MTAEHDAAIL PKPGGPLAVG KRATPEPGPN DVLIEVKAVA LNPCDYYQRD YGMPPVPIYP
AVIGGDAAGV VAKLGSSVTG GPVPGPGSRV IAFASSFYQN GSPDHGAFQK YALAQSEAVI
PLPDNLSFEE GAVFPLAVLT ALTAWTTIGI PLDTRYTPAD KQAVLIWGAS SSVGSFAVQS
AKTLGFTVYA TASPKHHELV KKLGADAVFD YKDSDVVSKI VDAVKKDGVY LHTAHCVVDG
ALQPTLDILK ETKGDAFAKV AHSPVLPECH PTLDNTQITF NFPSMDEVVR TRISKLRRAV
SRE
