TAZN_ASPTN
ID TAZN_ASPTN Reviewed; 456 AA.
AC Q0CS96;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Short chain dehydrogenase tazN {ECO:0000303|PubMed:35398258};
DE EC=1.1.1.- {ECO:0000305|PubMed:35398258};
DE AltName: Full=Azaphilone biosynthesis cluster protein N {ECO:0000303|PubMed:35398258};
GN Name=tazN {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03438;
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: Short chain dehydrogenase; 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 short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CH476597; EAU36712.1; -; Genomic_DNA.
DR RefSeq; XP_001212616.1; XM_001212616.1.
DR STRING; 33178.CADATEAP00010353; -.
DR EnsemblFungi; EAU36712; EAU36712; ATEG_03438.
DR GeneID; 4317482; -.
DR VEuPathDB; FungiDB:ATEG_03438; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_599882_0_0_1; -.
DR OrthoDB; 1194344at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..456
FT /note="Short chain dehydrogenase tazN"
FT /id="PRO_0000456070"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 44..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 71..72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 98..100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 195..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 227..229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 456 AA; 49926 MW; 549F27FEA797D80E CRC64;
MPPSKDQPNI LRGPGDYEVT TRVHNDTYPE IDPRLLNLQG KSVFVTGGSR GLGRSMALSF
AKAGVSKIAV GARSSLESLA KEIAEACVNP PEFLPVKLDV TDEASVAAAA TEVGRAFGQL
NVLVNNAGIL GKYGLIADSD PEEWWEVLNV NLRGPYLVTR AFVPLLLKAS KDDIRYIVNV
CSVGAHLTNP TLSSYQVSKN ALLKLTTLTN AEYGPGVITF AIHPGNSPTD IMGGPEAIPP
HHKHVFVETP ELSGDSVVFL VSKRREWLGG RYINCTWDLP ELVSKEAEIC IPVGLYQAKE
YVDIPFNGLR PEIDTAFQGR KQRTPEQARR AQLAKYNVVK GGMDNRRDSQ IFIRIKRSTK
HNPRLVRLVG NKSRPATSGI CRVDFFDCTA QKQRDKAQWQ SLKLSKAQVT GSVVTHLTQI
LSGNSQRTAG IQRARELGQI IWPLAAEQSD SGNSLP
