ID   ASTI_ASPOR              Reviewed;         201 AA.
AC   Q2UEL0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Sesquiterpene phosphatase astI {ECO:0000303|PubMed:27628599};
DE            EC=3.1.3.- {ECO:0000269|PubMed:27628599};
DE   AltName: Full=Astellolide biosynthesis cluster protein I {ECO:0000303|PubMed:27628599};
GN   Name=astI {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000576;
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, CATALYTIC ACTIVITY, 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: Sesquiterpene phosphatase; part of the gene cluster that
CC       mediates the biosynthesis of astellolides, drimane-type sesquiterpene
CC       esters that show antimicrobial, anti-inflammatory, and anti-tumor
CC       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   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP007159; BAE60005.1; -; Genomic_DNA.
DR   RefSeq; XP_001822007.1; XM_001821955.1.
DR   AlphaFoldDB; Q2UEL0; -.
DR   SMR; Q2UEL0; -.
DR   EnsemblFungi; BAE60005; BAE60005; AO090026000576.
DR   GeneID; 5994035; -.
DR   KEGG; aor:AO090026000576; -.
DR   VEuPathDB; FungiDB:AO090026000576; -.
DR   HOGENOM; CLU_045011_9_2_1; -.
DR   OMA; GIHGIVF; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..201
FT                   /note="Sesquiterpene phosphatase astI"
FT                   /id="PRO_0000450119"
SQ   SEQUENCE   201 AA;  22610 MW;  DBF6BBE4834DA1BA CRC64;
     MTRQSHYQAI ILDLGNVVFE WDTSQNPPTA APNQISLLRT SMKSPVYHSY ERGQLSTEEC
     HRLLGESLHV DPGQIKEAFD LARQSLRSNP ALLDFIRQLK QTRGVAVYAM SNIPQAEIEY
     LKESRAGDME VFDEVFASGY VGSRKPETEF YRRVMGEIGL KAERVVFVDD KEENVDVARG
     LGLYGVCFGG VEELRGHLLG I