ID   LUPS_BRUGY              Reviewed;         761 AA.
AC   A8CDT3;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Lupeol synthase;
DE            Short=BgLUS;
DE            EC=5.4.99.41;
GN   Name=LUS;
OS   Bruguiera gymnorhiza (Burma mangrove) (Rhizophora gymnorhiza).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Rhizophoraceae; Bruguiera.
OX   NCBI_TaxID=39984;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Leaf;
RX   PubMed=17803686; DOI=10.1111/j.1742-4658.2007.06025.x;
RA   Basyuni M., Oku H., Tsujimoto E., Kinjo K., Baba S., Takara K.;
RT   "Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae.";
RL   FEBS J. 274:5028-5042(2007).
CC   -!- FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of lupeol.
CC       {ECO:0000269|PubMed:17803686}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-epoxysqualene = lupeol; Xref=Rhea:RHEA:31383,
CC         ChEBI:CHEBI:6570, ChEBI:CHEBI:15441; EC=5.4.99.41;
CC         Evidence={ECO:0000269|PubMed:17803686};
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AB289586; BAF80444.1; -; mRNA.
DR   AlphaFoldDB; A8CDT3; -.
DR   SMR; A8CDT3; -.
DR   KEGG; ag:BAF80444; -.
DR   BioCyc; MetaCyc:MON-14452; -.
DR   BRENDA; 5.4.99.41; 1002.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0042299; F:lupeol synthase activity; IDA:UniProtKB.
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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11764; PTHR11764; 1.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   Pfam; PF13249; SQHop_cyclase_N; 1.
DR   SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
DR   TIGRFAMs; TIGR01787; squalene_cyclas; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Repeat.
FT   CHAIN           1..761
FT                   /note="Lupeol synthase"
FT                   /id="PRO_0000412990"
FT   REPEAT          148..189
FT                   /note="PFTB 1"
FT   REPEAT          639..680
FT                   /note="PFTB 2"
FT   ACT_SITE        484
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   761 AA;  87314 MW;  5F06DD537A7FFC89 CRC64;
     MWRLKIAEGG NNPYIYSTNN FVGRQTWEFD PEAGTPEERA QVEEARENFW RDRFLIKPSS
     DLLWRFQFLS EKKFKQRIPQ VKVQDGEEIT REIATTALRR SVHLVSALQA SDGHWCAENS
     GPMFFVPPMV FSLYITGHLN AVFSAEHCKE ILRYIYCHPN EDGGWGLHIE GHSAMFSTVL
     NYNWLGKLGE GRDGGKDNAC ERARRRILDH GSATAISSWG KTWLAILGVY EWDGCNPMPP
     EFWAFPTFFP IHPARMLCYC RLTYMAMSYL YGKKFVGPIT PLILQLREEI YNEPYDQINW
     SRMRHLCAKE DNYYAHTLTQ IILWDAIYML GEPLLKRWPF NKLREKALKI TMDHIHYEDE
     NSQYITIGSV EKPLLMLACW HEDPNGDAFK KHLARIPDYV WLGEDGIKIQ SFGSQVWDTS
     FVLQALIASN LPSETGPTLE KGHNFIKNSQ VTQNPSGDFR RMFRHISKGS WTFSDKDHGW
     QVSDCTAESL KCCLLFSMMP PELVGEKMGP QRMYDAVNVI ISLQSKNGGC SAWEPAGAGS
     WMEWLNPVEF LADLVIEHEY VECTSSSLQA LVLFKKLYPE HRRKEIEIFI LNAVRFTEEI
     QQPDGSWYGN WGICFLSGTW FGLKGLAAAG KTYYNCTAVR KGVEFLLQTQ RDDGGWGESY
     LSCPKKIYVP LEGNRSNLVQ TALAMMGLIL GGQGERDPTP LHRAAKLLIN SQTELGDFPQ
     QELSGCFMRN CMLHYSEYRD IFPTWALAEY CKLFPLPSKN D