ID   BRAA_ANNTR              Reviewed;         375 AA.
AC   P9WER0; A0A866WKL9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Terpene cyclase braA {ECO:0000303|PubMed:32936132};
DE            EC=4.2.3.- {ECO:0000269|PubMed:32936132};
DE   AltName: Full=Brasilane terpene glycosides biosynthesis cluster protein A {ECO:0000303|PubMed:32936132};
GN   Name=braA {ECO:0000303|PubMed:32936132};
OS   Annulohypoxylon truncatum (Hypoxylon truncatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Annulohypoxylon.
OX   NCBI_TaxID=327061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=DSM 103480 / CBS 140778;
RX   PubMed=32936132; DOI=10.1039/d0cc03950k;
RA   Feng J., Surup F., Hauser M., Miller A., Wennrich J.P., Stadler M.,
RA   Cox R.J., Kuhnert E.;
RT   "Biosynthesis of oxygenated brasilane terpene glycosides involves a
RT   promiscuous N-acetylglucosamine transferase.";
RL   Chem. Commun. (Camb.) 56:12419-12422(2020).
CC   -!- FUNCTION: Terpene cyclase; part of the gene cluster that mediates the
CC       biosynthesis of the brasilane terpene glycosides brasilane D and E
CC       (PubMed:32936132). The biosynthesis starts with the activity of the
CC       terpene cyclase braA that converts farnesyl pyrophosphate into the
CC       sesquiterpene alcohol trichobrasilenol (PubMed:32936132). Subsequently,
CC       trichobrasilenol is glycosylated by the O-glycosyltransferase braB
CC       putatively using UDP-GlcNAc as sugar donor to yield brasilane A
CC       (PubMed:32936132). The latter then undergoes two rounds of oxidation
CC       performed by the cytochrome P450 monooxygenase braC (PubMed:32936132).
CC       In the first round braC hydroxylates C-12 forming brasilane D, which
CC       serves as substrate in the second round to establish the epoxide at the
CC       bond between C-5 and C-10 and oxidize the alcohol at C-12 to an
CC       aldehyde leading to the final product brasilane E (PubMed:32936132).
CC       {ECO:0000269|PubMed:32936132}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9UR08};
CC       Note=Binds 3 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:Q9UR08};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32936132}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UR08}.
CC   -!- DOMAIN: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are
CC       required for coordinating the divalent metal ions that stabilize the
CC       PPi moiety of the substrate. {ECO:0000250|UniProtKB:Q9UR08}.
CC   -!- DOMAIN: The C-terminal WxxxxxRY motif is frequently found in terpene
CC       synthases and is important to guide product formation.
CC       {ECO:0000250|UniProtKB:P9WEY7}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; MT383109; QOE88883.1; -; Genomic_DNA.
DR   SMR; P9WER0; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034686; Terpene_cyclase-like_2.
DR   SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..375
FT                   /note="Terpene cyclase braA"
FT                   /id="PRO_0000453905"
FT   MOTIF           116..120
FT                   /note="D(D/E)XX(D/E) motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   MOTIF           264..272
FT                   /note="NSE motif"
FT                   /evidence="ECO:0000250|UniProtKB:P9WEY7"
FT   MOTIF           348..355
FT                   /note="WxxxxxRY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P9WEY7"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         354..355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ   SEQUENCE   375 AA;  43575 MW;  476A74E68C2474C4 CRC64;
     MAPDIDNIWS STTDAAESPV DERRILLKRA VGQKILVPSI LSLMPAWPSQ VHPAVDEVNT
     EIDKWLPTVN VAEKKKAKHR ARGNYAFLTA VYYPYCKETE RLVVIAKFLY WIFFWDDEID
     TGGELTEDEE GTIQCCEETN KCVDDCLGPN PNYNPPPNSR GTVEMFYPIL RDFRAGLGPV
     STERLRLELH DYINGVAKQQ KVRQGERLPD PWYHFKIRSD DVGVIPSITQ NEYAMKFELP
     EYVRRHEAME EIVQECTKLT VLLNDVLSLQ KEFRDSQLEN LVLLFMNRYN LSLQAAVDKV
     LDLIREHYAI CVAAEKRLPW SEDDEKLNDD IREYVRGCQR LATGTAYWSY SCERYFKQTQ
     VNDKWEVLLD LSYVE