ID   AURG_CALAK              Reviewed;         410 AA.
AC   A0A0M3STV6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Acetyltransferase aurG {ECO:0000303|PubMed:26340065};
DE            EC=2.3.1.- {ECO:0000269|PubMed:26340065};
DE   AltName: Full=Aurovertin biosynthesis cluster protein G {ECO:0000303|PubMed:26340065};
GN   Name=aurG {ECO:0000303|PubMed:26340065};
OS   Calcarisporium arbuscula (Dendryphion arbuscula).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Calcarisporium.
OX   NCBI_TaxID=240499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26340065; DOI=10.1021/jacs.5b07816;
RA   Mao X.M., Zhan Z.J., Grayson M.N., Tang M.C., Xu W., Li Y.Q., Yin W.B.,
RA   Lin H.C., Chooi Y.H., Houk K.N., Tang Y.;
RT   "Efficient biosynthesis of fungal polyketides containing the dioxabicyclo-
RT   octane ring system.";
RL   J. Am. Chem. Soc. 137:11904-11907(2015).
CC   -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of aurovertins, fungal polyketides that exhibit potent
CC       inhibition of adenosine triphosphate synthase (PubMed:26340065). Tha
CC       biosynthesis starts with the HR-PKS aurA that selects propionate as the
CC       starter unit; synthesizes a hexa-ene chain through the repeated
CC       functions of the KR and DH domains in the first six iterations;
CC       selectively introduces three alpha-methyl substitutions at C4, C6, and
CC       C16 using the S-adensylmethionine-dependent cMET; and shuts off KR and
CC       DH in the last three iterations to afford a 1,3,5-triketo portion that
CC       can undergo intramolecular cyclization to yield the alpha-pyrone
CC       intermediate (PubMed:26340065). AurE may act as a cyclase and enhances
CC       the rate of pyrone formation and product release of aurA
CC       (PubMed:26340065). The methyltransferase aurB then methylates the C17
CC       hydroxyl group (PubMed:26340065). C17 methylation is required to
CC       initiate epoxidation by the downstream monooxygenase aurC
CC       (PubMed:26340065). The monooxygenase aurC and the epoxide hydrolase
CC       aurD can iteratively transform the terminal triene portion of the
CC       methylated precursor into the dioxabicyclo[3.2.1]octane scaffold of
CC       aurovertin E. Epoxidation modifications of the precursor occur in two
CC       separate steps; bis-epoxidation of the two terminal olefins takes place
CC       first, followed by another epoxidation that occurs at C7-C8 after
CC       tetrahydrofuran formation (PubMed:26340065). The O-acyltransferase aurG
CC       converts aurovertin E to aurovertin A (PubMed:26340065).
CC       {ECO:0000269|PubMed:26340065}.
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:26340065}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Accumulates autovertin E but does not produce its
CC       acetylated form aurovertin A (PubMed:26340065).
CC       {ECO:0000269|PubMed:26340065}.
CC   -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR   EMBL; KT581580; ALD83633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M3STV6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR044851; Wax_synthase.
DR   InterPro; IPR032805; Wax_synthase_dom.
DR   PANTHER; PTHR31595; PTHR31595; 1.
DR   Pfam; PF13813; MBOAT_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycoprotein; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..410
FT                   /note="Acetyltransferase aurG"
FT                   /id="PRO_0000443971"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          90..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   410 AA;  45987 MW;  EB714CCBA36952E4 CRC64;
     MGLWLVLANQ VGLVGTLVLV VCFTPANSLV RPLLLPGITA LVSYGLILNK EAIANAGAWS
     LVNLNTAGLF LQYLDVGLIS RWTYSAYGPT SSRGGQPNAS LDLAGRKKPP SSSLLSRLQW
     GFSTATSWRA PSTVWEAKGT PHFEELPSRG RFLARNAMTL LWSVLVLDVM GLVGGDLDPV
     ANAAHFTWDR VRFLARLGDV SRDEVILRAT VVYMRWGAMY FSLQVVYSFL AIVFVMVGLS
     PVQRWPPLFG SFTEIYTLRN TWGKAWHQLI RQKVSSPAHY TTYSLLGLRK GGIAGRYTCI
     LATFFVSGLL HLFCAEYSYG IQWDQSGTLR FYSIQALGIA MEDAVQATSR RLFAYRSTYW
     TRAIGYVWVL LWFLWTSPAY FFPLLKYDTE KRPPVLLGPI ETWLQSRHVQ