ID   LUPS_KALDA              Reviewed;         765 AA.
AC   E2IUA9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Lupeol synthase;
DE            Short=KdLUS;
DE            EC=5.4.99.41;
OS   Kalanchoe daigremontiana (Devil's backbone) (Bryophyllum daigremontianum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Saxifragales; Crassulaceae; Kalanchoe.
OX   NCBI_TaxID=23013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20610397; DOI=10.1074/jbc.m109.098871;
RA   Wang Z., Yeats T., Han H., Jetter R.;
RT   "Cloning and characterization of oxidosqualene cyclases from Kalanchoe
RT   daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding
RT   friedelin and other triterpenoids.";
RL   J. Biol. Chem. 285:29703-29712(2010).
CC   -!- FUNCTION: Oxidosqualene cyclase that generates lupeol, a triterpenoid
CC       product. Lupeol is probably required to coat the leaf exterior as a
CC       defense compound against pathogens or herbivores.
CC       {ECO:0000269|PubMed:20610397}.
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:20610397};
CC   -!- TISSUE SPECIFICITY: Expressed only in the epidermal cells on both sides
CC       of the leaf and not in internal leaf tissues.
CC       {ECO:0000269|PubMed:20610397}.
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
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DR   EMBL; HM623871; ADK35126.1; -; mRNA.
DR   AlphaFoldDB; E2IUA9; -.
DR   SMR; E2IUA9; -.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
DR   GO; GO:0042299; F:lupeol synthase activity; IEA:UniProtKB-EC.
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   SFLD; SFLDG01016; Prenyltransferase_Like_2; 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..765
FT                   /note="Lupeol synthase"
FT                   /id="PRO_0000418481"
FT   REPEAT          148..189
FT                   /note="PFTB 1"
FT   REPEAT          640..681
FT                   /note="PFTB 2"
FT   ACT_SITE        485
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   765 AA;  87975 MW;  FBA2A79C30558B7C CRC64;
     MWKLKIADGG SNPYIFTTNN FVGRQIWEFD PQATDPQQLA KVEAARLDFY HNRYKLKPNS
     DLLWRMQFLE EKAFTQTIPQ VKVEDGEEVS YEAVTAALRR GVHLYSALQA SDGHWPAENA
     GPMFFMPPMV MCLYITGHLN AIFTEEHRSE TLRYIYYHQN EDGGWGFHIE GHSTMFGTVL
     NYICMRLLGE GPEGGQDNAV SRGRKWILDH GGATSIPSWG KTWLSIMGLC DWSGCNPMPP
     EFWLLPSYLP MHPGKMWCYC RMVYMPMSYL YGKRFTARIT PLILQLREEI HIQPYDQIDW
     KKVRHVCCKE DMYYPHPLLQ DLLWDTLYLT TEPLLTRWPL NKLIRKRALQ TTMKHIHYED
     ENSRYITIGC VEKVLCMLAC WVEDPNGDYF KKHLARIPDY LWIAEDGMKM QSFGSQHWDT
     AFSIQALLAS NMAEEIGITL AKGHDFIKKS QVKDNPSGDF KGMYRHISKG AWTFSDQDHG
     WQVSDCTAEG LKCCLLFSMM QPEVVGESMA PESLYNSVNV LLSLQSQNGG LPAWEPAGAP
     EWLELLNPTE FFENIVIEHE YVECTSSAVQ ALVLFKKLYP LHRRKEVERF ITNGAKYLED
     IQMPDGSWYG NWGVCFTYGA WFALEGLSAA GKTYNNCAAV RKGVDFLLNI QLEDGGWGES
     YQSCPDKKYV PLEDNRSNLV QTSWALMGLI YAGQADRDPT PLHRAAQLLI NSQLEDGDFP
     QQEITGVFQR NCMLHYAAYR NIFPLWALAE YRRQIQLHSE ATKMV