ID   AURD_CALAK              Reviewed;         383 AA.
AC   A0A0M4KRN2;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Terpene cyclase aurD {ECO:0000303|PubMed:26340065};
DE            EC=5.4.99.- {ECO:0000269|PubMed:26340065};
DE   AltName: Full=Aurovertin biosynthesis cluster protein D {ECO:0000303|PubMed:26340065};
GN   Name=aurD {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], AND FUNCTION.
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: Epoxide hydrolase; 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   -!- SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family.
CC       {ECO:0000305}.
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DR   EMBL; KT581577; ALD83630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4KRN2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Isomerase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..383
FT                   /note="Terpene cyclase aurD"
FT                   /id="PRO_0000443968"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   383 AA;  43009 MW;  224003E3F29FD9B9 CRC64;
     MPQSTKYILP VYGILALYSL GYFSYRNGYV NIVLEERQAW LDMPPGDPTK VAQPTGIASL
     DETLAAMFVF YWPVLDGSFP GLSLMFCNYL GALPLCLVLM TLESLRKGNR SSFSFFYSPT
     FWGMIAVMMT LAVSIPWYLT IHLLISTTAS HPTIENMSIP LAELKALIVN IVVGLVLPSL
     LVALPETITQ TLFTRQTAIT LWQLWPFWST AVHFIARKFI SATERGADSR AQWTRVRSAF
     RSVYGLTFAA AAIAHIATWS ISLTAAYALP DAMSAETVSS LHPQTVFVNT WPWLPVTTDS
     VGEGTLWLLQ WDKFVGVGAI YWWSLDLYRA AHTAQRKKIN WYYFALKTVA FCLVSGFTGA
     TIELLWEREE MIMEAGRAKE KTK