ID   LCC_LYCCL               Reviewed;         756 AA.
AC   A0A125SXN1;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Pre-alpha-onocerin synthase LCC {ECO:0000303|PubMed:26663356};
DE            EC=5.4.99.65 {ECO:0000269|PubMed:26663356};
GN   Name=LCC {ECO:0000303|PubMed:26663356};
OS   Lycopodium clavatum (Stag's-horn clubmoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Lycopodiales; Lycopodiaceae; Lycopodioideae; Lycopodium.
OX   NCBI_TaxID=3252;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=26663356; DOI=10.1002/cbic.201500663;
RA   Araki T., Saga Y., Marugami M., Otaka J., Araya H., Saito K., Yamazaki M.,
RA   Suzuki H., Kushiro T.;
RT   "Onocerin biosynthesis requires two highly dedicated triterpene cyclases in
RT   a fern Lycopodium clavatum.";
RL   ChemBioChem 17:288-290(2016).
CC   -!- FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of alpha-
CC       onocerin, a triterpenoid characterized by a symmetrical structure due
CC       to cyclizations at both termini of dioxidosqualene that inhibits
CC       acetylcholinesterase. Catalyzes the first half of the cyclization,
CC       exclusively from dioxidosqualene. {ECO:0000269|PubMed:26663356}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene = pre-
CC         alpha-onocerin; Xref=Rhea:RHEA:54664, ChEBI:CHEBI:138305,
CC         ChEBI:CHEBI:138307; EC=5.4.99.65;
CC         Evidence={ECO:0000269|PubMed:26663356};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:26663356}.
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LC053635; BAU46471.1; -; mRNA.
DR   AlphaFoldDB; A0A125SXN1; -.
DR   SMR; A0A125SXN1; -.
DR   KEGG; ag:BAU46471; -.
DR   BRENDA; 5.4.99.65; 3106.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
DR   GO; GO:0016104; P:triterpenoid biosynthetic process; IDA:UniProtKB.
DR   CDD; cd02892; SQCY_1; 1.
DR   InterPro; IPR032696; SQ_cyclase_C.
DR   InterPro; IPR032697; SQ_cyclase_N.
DR   InterPro; IPR018333; Squalene_cyclase.
DR   InterPro; IPR002365; Terpene_synthase_CS.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11764; PTHR11764; 1.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   Pfam; PF13249; SQHop_cyclase_N; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
DR   TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR   PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Repeat.
FT   CHAIN           1..756
FT                   /note="Pre-alpha-onocerin synthase LCC"
FT                   /id="PRO_0000445704"
FT   REPEAT          96..138
FT                   /note="PFTB 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          146..187
FT                   /note="PFTB 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          438..491
FT                   /note="PFTB 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          512..554
FT                   /note="PFTB 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          589..629
FT                   /note="PFTB 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          638..679
FT                   /note="PFTB 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          700..747
FT                   /note="PFTB 7"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        483
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            416
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            610
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   756 AA;  86189 MW;  B40C6F86045D51BA CRC64;
     MWKLKIAEGS PGLDTLNDHV GRQIWCYEKD AGTPEEHAEV EEARAKFTEQ RHEQRQSADI
     LMKLQLLKEN SFSPLPTQPK VDRFEDITED AVQTTLRRAL RFFAAIQAHD GHWPGDHAGL
     MFLTPCLVIC LYVTGALNTV LSEAHRQEMR RYLYNHQNKD GGWGLNIESH STMFCTVFSY
     VTLRLLEEGP HDGDEGAMES ARLWILDHGG AIAIPSWGKF WLAVLGVFEW SGVHPMPPEI
     WFLPHFLPIH PGQMNIHGKL ILLPMTYIYG RQFVGPITSL VKALRGEIFS THYNTIDWQE
     ARTMCAKEDR YYSTPFVQDL AFTFAKQCTE PLLRSWPGSL VRKKALERVI KWIHTEDKNF
     RYVGIGPLSK VSVMLCCWIE DPNSEAFKRH LLRVHDYLWL AEDGMKMQGY NGCQMWETVL
     GTQAVLSARM HDECNSMLRK AEDYISKTQI QEDGNLDTKL WYHKISKGGW PHSTRDHGWP
     ISDCSAEGLK VALALADLPW AMTGSQISEE NLFDCVNVIL SLQNPDGGFS AFELKRAYPW
     AEKLLQSETF GDITIDYSWV ECSSSCIQAL VAFKKKYTTH RKEEICRAIN RACRFIESIQ
     RKDGSWYGYW AVCFTYGAWF GITGLVAAGK SFHESEAIRR ACDFLLSKQL PSGGWGESYL
     SSENEEYTHL KHGRAHVVHT AWSLLALLAS GQAERDPVPL HRAATILINS QLENGDYPQQ
     EIVGAIHKTC MTTYTLFCNI FAIQALGEYR QKIFHS