ID   ANDG_EMEVA              Reviewed;         481 AA.
AC   A0A097ZPE2;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=O-acetyltransferase andG {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000269|PubMed:25216349};
DE   AltName: Full=Anditomin synthesis protein G {ECO:0000303|PubMed:25216349};
GN   Name=andG {ECO:0000303|PubMed:25216349};
OS   Emericella variicolor (Aspergillus stellatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1549217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX   PubMed=25216349; DOI=10.1021/ja508127q;
RA   Matsuda Y., Wakimoto T., Mori T., Awakawa T., Abe I.;
RT   "Complete biosynthetic pathway of anditomin: nature's sophisticated
RT   synthetic route to a complex fungal meroterpenoid.";
RL   J. Am. Chem. Soc. 136:15326-15336(2014).
CC   -!- FUNCTION: O-acetyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of anditomin, a fungal meroterpenoid
CC       (PubMed:25216349). The first step of the pathway is the synthesis of
CC       3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM
CC       (PubMed:25216349). DMOA is then converted to the phthalide compound
CC       5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450
CC       monooxygenase andK, which is further prenylated by the
CC       prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349).
CC       Further epoxidation by the FAD-dependent monooxygenase andE leads to
CC       epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the
CC       terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid
CC       A through opening of the epoxide ring followed by the cyclization of
CC       the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn
CC       oxidized at the C-3 hydroxyl group to yield preandiloid B by the
CC       dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely
CC       responsible for the dehydrogenation of preandiloid B leading to the
CC       enone preandiloid C, as well as for the intriguing structural
CC       rearrangement to generate the bicyclo[2.2.2]octane core, transforming
CC       preandiloid C into andiconin (PubMed:25216349). FAD-binding
CC       monooxygenase andJ then produces andilesin D which is reduced by
CC       dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of
CC       acetyltransferase andG followed by a spontaneous acetate elimination
CC       leads then to andilesin B, which is in turn substrate of the short
CC       chain dehydrogenase andH to yield andilesin C (PubMed:25216349).
CC       Finally, the dioxygenase andF catalyzes the transformation of andilesin
CC       C to anditomin (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:25216349}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4WZ64}.
CC   -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB981314; BAP81861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097ZPE2; -.
DR   SMR; A0A097ZPE2; -.
DR   BioCyc; MetaCyc:MON-19054; -.
DR   UniPathway; UPA00213; -.
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   1: Evidence at protein level;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..481
FT                   /note="O-acetyltransferase andG"
FT                   /id="PRO_0000436583"
SQ   SEQUENCE   481 AA;  53368 MW;  9DE9531A1A9B71C4 CRC64;
     MPGFQSLRLD VLSPVDHSFP DYNPCYYLYF RSPSASDVRT SLQRGLEKLI KILPFITGEV
     VPCDGDRMEK RNGLLCIKYT ASPDESLPII EFREDMSLSV ENISTSKTRT GLEDVHLAKT
     LAPLPLTPNP SRPSYVVRFR ATTVRDGVVL AMSFSHFVFD ATGAGHLMEH FAECVREPEP
     KPCDIDQETL RQALWHINGD TGVIPNEPGD CHSLPAFMLP PGGREAIPEM AAPGMRVCRW
     KISAAKVELL KNTCNDLLRS LDYKAGDNSV NFLSSQDVLT GLLTTCLKHD PKGKVEGSDI
     GVAVNLRNRL SPEWPTGYFG NMAKYAIAPG LAEPTAEELA VAHRLVAENP KILPAASDIA
     RLYRNACSIR HTISQISDVH IRGFVSWLNS CKDLGPLTTP FPFINFTSWR HLNLYELDFG
     GALGYVDDIQ THGMMPTLGI ILPRAKAVQG TEAHWDVLFY VKNEDYPAVM KQGLLRFLTV
     D