ASTE_ASPOR
ID ASTE_ASPOR Reviewed; 261 AA.
AC Q2UEK6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Short chain dehydrogenase/reductase astE {ECO:0000303|PubMed:27628599};
DE EC=1.1.-.- {ECO:0000305|PubMed:27628599};
DE AltName: Full=Astellolide biosynthesis cluster protein E {ECO:0000303|PubMed:27628599};
GN Name=astEA {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000580;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=27628599; DOI=10.1038/srep32865;
RA Shinohara Y., Takahashi S., Osada H., Koyama Y.;
RT "Identification of a novel sesquiterpene biosynthetic machinery involved in
RT astellolide biosynthesis.";
RL Sci. Rep. 6:32865-32865(2016).
CC -!- FUNCTION: Short chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of astellolides, drimane-type
CC sesquiterpene esters that show antimicrobial, anti-inflammatory, and
CC anti-tumor activities (PubMed:27628599). The first step in astellolide
CC biosynthesis is performed by the sesquiterpene cyclase astC that
CC catalyzes the formation of drimanyl pyrophosphate from farnesyl
CC pyrophosphate (PubMed:27628599). Drimanyl pyrophosphate is then
CC dephosphorylated by the sesquiterpene phosphatase astI to produce
CC drimanyl monophosphate which is further dephosphorylated to drim-8-ene-
CC 11-ol by atsK (PubMed:27628599). Drim-8-ene-11-ol is converted to
CC confertifolin, probably by the cytochrome P450 monooxygenase astD
CC and/or the dehydrogenase astE (PubMed:27628599). The cytochrome P450
CC monooxygenases astB, astF and astJ then hydroxylate confertifolin at
CC C6, C14, or C15 to form trihydroxy confertifolin (PubMed:27628599). The
CC nonribosomal peptide synthetase astA catalyzes ester bond formation
CC between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy
CC benzoic acid (4HBA), leading to the formation of dideacetyl
CC astellolides A and B, respectively (PubMed:27628599). Finally, the O-
CC acetyltransferase astG converts dideacetyl astellolides A and B into
CC deacetyl astellolides A and B (PubMed:27628599).
CC {ECO:0000269|PubMed:27628599}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:27628599}.
CC -!- INDUCTION: Expression is regulated by the secondary metabolite
CC regulator cclA. {ECO:0000269|PubMed:27628599}.
CC -!- DISRUPTION PHENOTYPE: Significantly reduces the production of deacetyl
CC astellolides A and B. {ECO:0000269|PubMed:27628599}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AP007159; BAE60009.1; -; Genomic_DNA.
DR RefSeq; XP_001822011.1; XM_001821959.1.
DR AlphaFoldDB; Q2UEK6; -.
DR SMR; Q2UEK6; -.
DR STRING; 510516.Q2UEK6; -.
DR EnsemblFungi; BAE60009; BAE60009; AO090026000580.
DR GeneID; 5994039; -.
DR KEGG; aor:AO090026000580; -.
DR VEuPathDB; FungiDB:AO090026000580; -.
DR HOGENOM; CLU_010194_1_0_1; -.
DR OMA; NMLPIPW; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..261
FT /note="Short chain dehydrogenase/reductase astE"
FT /id="PRO_0000450120"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 16..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 43..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 69..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 164..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 197..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 261 AA; 27157 MW; 0C8070B6562CE098 CRC64;
MTGNEQKFSL QGKVAIVTGA GSGIGRETAL CLANAGANVV VAEANETTGK ETAAKVSAQT
GSRGLFILTD VSRSESVQAM VIATIEAFGR LDIAVNNAAL HPDASPIAEL HEDHWQKIIG
VNLVGVAFCL KWELQQMIQQ GGGGSIINIS SATINRPQEK MSAYIAAKHG ITGLTQTAAV
ENGRHGIRVN ALAPGGVATD LTMATMQELG LTEENEAARS SLFKRFAKPE EIAQSVLWLA
SDAASYVTGA TIAVDSGLSL I
