ID   ASTC_ASPOR              Reviewed;         291 AA.
AC   Q2UEK4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Sesquiterpene cyclase astC {ECO:0000303|PubMed:27628599};
DE            EC=4.2.3.- {ECO:0000269|PubMed:27628599};
DE   AltName: Full=Astellolide biosynthesis cluster protein C {ECO:0000303|PubMed:27628599};
GN   Name=astC {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000582;
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 cyclase; part of the gene cluster that mediates
CC       the biosynthesis of astellolides, drimane-type sesquiterpene esters
CC       that show antimicrobial, anti-inflammatory, and anti-tumor activities
CC       (PubMed:27628599). The first step in astellolide biosynthesis is
CC       performed by the sesquiterpene cyclase astC that catalyzes the
CC       formation of drimanyl pyrophosphate from farnesyl pyrophosphate
CC       (PubMed:27628599). Drimanyl pyrophosphate is then dephosphorylated by
CC       the sesquiterpene phosphatase astI to produce drimanyl monophosphate
CC       which is further dephosphorylated to drim-8-ene-11-ol by atsK
CC       (PubMed:27628599). Drim-8-ene-11-ol is converted to confertifolin,
CC       probably by the cytochrome P450 monooxygenase astD and/or the
CC       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; BAE60011.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UEK4; -.
DR   SMR; Q2UEK4; -.
DR   EnsemblFungi; BAE60011; BAE60011; AO090026000582.
DR   HOGENOM; CLU_045011_9_2_1; -.
DR   OMA; CSQGLHG; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0016829; F:lyase 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; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..291
FT                   /note="Sesquiterpene cyclase astC"
FT                   /id="PRO_0000450118"
SQ   SEQUENCE   291 AA;  32794 MW;  B1909942DE2D02BD CRC64;
     MTKINPYKGI LVELKDIVFT SSSDQIKLPI NTFKSILCCG ATAQYQCGKI NRAQYYSRLA
     RDFALSLADV TALFDTVQAT IRPEESFLAF LAELKSRFGE QLKLYAVANM SREDYAMLKS
     LPIDWSLFDG VFLSADLGMR KPELRFFRHV LESISMKPED TILVDNDTDN ILCALSMGLK
     GILFGSTSVP QALTNLLEYD HISRAEQFLR SHAKSLHSVT HTGVTIRENF AQLLILEATG
     DIDLVELEYH PTTWNYFIGT QSSQLLLHKH NADRMTTMTS CWLVSAFLVV S