TAZHJ_ASPTN
ID TAZHJ_ASPTN Reviewed; 698 AA.
AC Q0CS91;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Dual trans-enoyl reductase/FAD-dependent monooxygenase tazHJ {ECO:0000303|PubMed:35398258};
DE EC=1.-.-.- {ECO:0000305|PubMed:35398258};
DE AltName: Full=Azaphilone biosynthesis cluster protein HJ {ECO:0000303|PubMed:35398258};
GN Name=tazHJ {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03443;
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, DISRUPTION PHENOTYPE, 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: Dual trans-enoyl reductase/FAD-dependent monooxygenase; part
CC of the gene cluster that mediates the biosynthesis of azaterrilone A
CC and other azaphilones, a class of fungal metabolites characterized by a
CC highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad
CC range of bioactivities (PubMed:35398258). The first step of the pathway
CC begins with the non-reducing polyketide synthase tazA that assembles
CC one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a
CC series of Claisen condensations, methylation, PT-mediated cyclization,
CC and finally releases the first hexaketide precursor through the R-
CC domain. The tazA product then undergoes reduction on its terminal
CC ketone and the following pyran-ring formation by yet undetermined
CC enzyme(s). Dehydration and enoyl reduction, possibly involving the
CC trans-enoyl reductase tazE leads to the next intermediate. TazD is
CC predicted as an acetyltransferase and might catalyze the acetylation
CC steps leading to the synthesis of azaterrilone A. Azaterrilone A is not
CC the final product of the taz pathway and both the highly reducing
CC polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps
CC of the pathway, leading to the production of the 2 final stereoisomers
CC that contain additional polyketide modification whose structures have
CC still to be determined (Probable). {ECO:0000269|PubMed:35398258,
CC ECO:0000305|PubMed:35398258}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:35398258}.
CC -!- INDUCTION: Expression is positively regulated by the azaterrilone A
CC cluster-specific transcription factor tazR.
CC {ECO:0000269|PubMed:35398258}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the accumulation of azaterrilone
CC A. {ECO:0000269|PubMed:35398258}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc-containing
CC alcohol dehydrogenase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the paxM FAD-
CC dependent monooxygenase family. {ECO:0000305}.
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DR EMBL; CH476597; EAU36717.1; -; Genomic_DNA.
DR RefSeq; XP_001212621.1; XM_001212621.1.
DR STRING; 33178.CADATEAP00010359; -.
DR EnsemblFungi; EAU36717; EAU36717; ATEG_03443.
DR GeneID; 4317487; -.
DR VEuPathDB; FungiDB:ATEG_03443; -.
DR eggNOG; KOG1198; Eukaryota.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_394806_0_0_1; -.
DR OMA; ELSHVIC; -.
DR OrthoDB; 521070at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..698
FT /note="Dual trans-enoyl reductase/FAD-dependent
FT monooxygenase tazHJ"
FT /id="PRO_0000456074"
FT BINDING 54..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 78..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 96
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 279..280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 299..300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 571
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 581..585
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 698 AA; 76638 MW; 874D4FB543418730 CRC64;
MLIIQIPDGM PDEDACTLGV GITTVGQGLY QSLGLPLPGS RARANFPILI YGGSTATGSL
AIQYARLSGC SQIITTCSPR HFDWAKSLGA DASFDYRDPD CVQKIKDCTQ NTLAHVLDCV
STSASAELCA AAIGSNGGTV SYLLPLKHQR EDVEAKYTLA YTAFGEYFSI AGTRKFEARP
EDLEFAKMFW KLSEGLVAEG KIRVHPPRVG KDGLKGVLDG FQAMREGQNW IPNMYGYEVG
DECRSLHVWA DRRSLEIPRA PIDQNATSNL DVAIVGGGIA GVTLALGLLK RGIKPIIYER
GRSFREIGAG IGFTPNAEWA MKVLDPEIHA AFKRVTVQNG TDWFIWMDGS LEKEAVVHKM
YLGERGFEGC ARADFLDELV KSLPQGTVRF SKNLVDIVDE DGASEVRLKF SDGSTASAHI
VIGCDGIRSK VRQFVIGGDD QPAHHPHYTH KYAFRGLVPM DKAYAALGQE KTDTRHMYLG
PDAHALTFPV AGGKLLNVVA FVTDPSSWPD GEKFTLPASK TDAVKAFERF NSTVRAIIDM
LPEELSRWAV FDTYDYPAPT FVRGRVCISG DAAHAAAPYH GAGAGFAVED AAVLAELLSD
AYDYLKISDV EKADIPKSVV LRKALETYNS IRLERAHWLV ETSRHIGEIY EGQNADIGLD
HTKCAAEIDW RCRKIWDYDV DDMMKQTSTL FKKQLGMI
