ID   ASTG_ASPOR              Reviewed;         471 AA.
AC   Q2UEK8;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=O-acetyltransferase astG {ECO:0000303|PubMed:27628599};
DE            EC=2.3.1.- {ECO:0000269|PubMed:27628599};
DE   AltName: Full=Astellolide biosynthesis cluster protein G {ECO:0000303|PubMed:27628599};
GN   Name=astGA {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000578;
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: O-acetyltransferase; 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   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4WZ64}.
CC   -!- INDUCTION: Expression is regulated by the secondary metabolite
CC       regulator cclA. {ECO:0000269|PubMed:27628599}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of deacetyl astellolides A
CC       and B and leads to the accumulation of dideacetyl astellolides A and B.
CC       {ECO:0000269|PubMed:27628599}.
CC   -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AP007159; BAE60007.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UEK8; -.
DR   SMR; Q2UEK8; -.
DR   EnsemblFungi; BAE60007; BAE60007; AO090026000578.
DR   VEuPathDB; FungiDB:AO090026000578; -.
DR   HOGENOM; CLU_026450_1_1_1; -.
DR   OMA; ILPRMYF; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..471
FT                   /note="O-acetyltransferase astG"
FT                   /id="PRO_0000450121"
SQ   SEQUENCE   471 AA;  52449 MW;  2E83360003A1CE17 CRC64;
     MGEQTEFEPI QLSPLDQAIP PVYIRILLCF SVVNVDRAIS QLQTGVSSLL SALPFLSGDV
     VRYTAPGKTK WLYQLCPPTH QVQATGVLVV KHHQMRCMVD EKRFAPSSTS HIPLSPFAEP
     ARPAPIFRVQ ANAYIDGITL GFAFHHIAVD ATGMGVIISE LARHCRSSPP PSLLCPDYER
     ATRQLISNSR ATECSGLDHS GDYISCQALS PPAEGSEDAS PSIEISTETR TFVFPAARLE
     SLKNACIEML PTLDQQQRQQ NPCLDEPART KVPWLSTNDV FVALLWVCLT RCRYQEDQNS
     GLPSDEHTRI CMGVNMRSRI QPPLSADYLG NAILSLSFKL NVNVFRRTQV TNESIEGVDS
     KDIEHKQWLA TICRVARNIR RGVNGMDDSY FRSVVSFLED SSDCRLFDYA RCDFCVPSWR
     HLCVYHADFG EMGRPKSLEV FDVPGDGSFC ILPQHYGAAA PWELLLGLLK A