ID   GLUTS_KALDA             Reviewed;         767 AA.
AC   E2IUA7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Glutinol synthase;
DE            Short=KdGLS;
DE            EC=5.4.99.49;
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 glutinol, a triterpenoid
CC       product. Glutinol 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 = glutinol; Xref=Rhea:RHEA:31859,
CC         ChEBI:CHEBI:15441, ChEBI:CHEBI:63462; EC=5.4.99.49;
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; HM623869; ADK35124.1; -; mRNA.
DR   AlphaFoldDB; E2IUA7; -.
DR   SMR; E2IUA7; -.
DR   KEGG; ag:ADK35124; -.
DR   BioCyc; MetaCyc:MON-17973; -.
DR   BRENDA; 5.4.99.49; 2798.
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; 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..767
FT                   /note="Glutinol synthase"
FT                   /id="PRO_0000418482"
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   767 AA;  88148 MW;  C19EE928D94D71D0 CRC64;
     MWKLKIADGG SNPYIFTTNN FVGRQIWEFD PQATDPQQLA KVEAARLDFY HNRYKLKPNS
     DLLWRMQFLE EKDFRQNIPQ 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 NKLIRQRALQ KTMKHIHYED
     ENSRYITIGT VEKVLCMLAC WVEDPNGDYF KKHLARVPDY FWVAEDGMKI QSFGSQHWDT
     VFSAQALLAS DMADEIGTTL AKAHYCIKES QVKDNPSGDF RSMYRHISKG SWTFSDQDHG
     WQLSDCTAEG LKCCLLFSLM QPEVVGEAMP PERLFDSVNI LLYLQSKNGG MPGWEPAGAS
     EWLELLNPTE FFENIVIEHE YVECTSSAVQ ALVLFKKLHP GHRRKEVERF ITNGAKYIED
     IQMPDGAWYG NWGVCFTYGA WFALGGLAAA GKTYNNCAAV RKGVDFLLRI QLEDGGWGES
     YQSCPDKKYV PLEDNRSNLV HTSWALMGLL CSGQADRDPN PLHRAAKLLI NSQLEDGDFP
     QQEITGVFKM NCMLHFAAYR SIFPVWALAE YKRFCNLSSE AISKPSK