ID   TARS_KALDA              Reviewed;         779 AA.
AC   E2IUA6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Taraxerol synthase;
DE            Short=KdTAS;
DE            EC=5.4.99.35;
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 taraxerol, a
CC       triterpenoid product. Taraxerol is probably required to coat the leaf
CC       exterior as a defense compound against pathogens or herbivores.
CC       {ECO:0000269|PubMed:20610397}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-epoxysqualene = taraxerol; Xref=Rhea:RHEA:30431,
CC         ChEBI:CHEBI:9402, ChEBI:CHEBI:15441; EC=5.4.99.35;
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; HM623868; ADK35123.1; -; mRNA.
DR   AlphaFoldDB; E2IUA6; -.
DR   SMR; E2IUA6; -.
DR   BioCyc; MetaCyc:MON-17976; -.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0016866; F:intramolecular transferase 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; 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..779
FT                   /note="Taraxerol synthase"
FT                   /id="PRO_0000418480"
FT   REPEAT          167..208
FT                   /note="PFTB 1"
FT   REPEAT          659..700
FT                   /note="PFTB 2"
FT   ACT_SITE        504
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   779 AA;  89734 MW;  54BFFFCCDD7D7BD5 CRC64;
     MSFVWVEESK ECSEQRKGSM WKLKIAQGGK DPYLYSTNNY VGRQTWEFDP EAGTPEERAE
     VEAARLNFYN NRYRVKPSAD LLYRMQFLKE KNFKQTIPPV KVEDGEEITY ETATTALKRA
     VHFYSALQAS DGHWPAENSG PLFFLPPLVM CLYITGHLNT VFPAEHQREI LRYIYYHQNE
     DGGWGLHIEG HSTMFCTALS YICMRILGEG PDGGLDNAVA RGRKWILDHG TVTAMPSWGK
     TWLSIMGLFD WSGSNPMPPE FWLLPSFLPM YPAKMWCYCR MVYMPMSYLY GKRFVGPITP
     LILQLREELY DQPYEQVNWK QVRHECAKED IYYPHPKIQD LLWDTLYIAI EPLLTRWPFN
     KLVRERALQR TMKHIHYEDE NSRYITIGCV EKVLCMLACW VEDPNGDYFK KHLARVPDYI
     WVAEDGMKMQ SFGSQQWDTG FAIQALLASN MSDEIGETLA KGHDFVKKSQ VKDNPSGDFK
     SMHRHISKGS WTFSDQDHGW QVSDCTAEGL KCCLLFSLMP PELVGEKMEP ERLYDSVNIL
     LSLQSKNGGL AAWEPAGAPE WLELLNPTEF FADIVIEHEY VECTASAIQA LVLFKKLYPG
     HRKKDIETFI KGAAQYIEDR QMPDGSWYGS WGVCFTYGTW FALGGLAAAG KNYDNCAAIR
     KGTEFLLNTQ CENGGWGESY RSCPEKRYVP LEENKSNLVH TAWALMGLIH SRQAERDITP
     LHRAAKLLIN SQLENGDFPQ QEITGVFMKN CMQHYAAYRN IYPLWGIAEY RKQIPLPLR