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 27-MAR-2024, entry version 43. 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}. 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; HM623869; ADK35124.1; -; mRNA. DR AlphaFoldDB; E2IUA7; -. DR SMR; E2IUA7; -. DR KEGG; ag:ADK35124; -. DR BioCyc; MetaCyc:MONOMER-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 Gene3D; 1.50.10.20; -; 2. DR InterPro; IPR032696; SQ_cyclase_C. DR InterPro; IPR032697; SQ_cyclase_N. DR InterPro; IPR018333; Squalene_cyclase. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR NCBIfam; TIGR01787; squalene_cyclas; 1. DR PANTHER; PTHR11764:SF58; BETA-AMYRIN SYNTHASE-RELATED; 1. DR PANTHER; PTHR11764; TERPENE CYCLASE/MUTASE FAMILY MEMBER; 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; Terpenoid cyclases/Protein prenyltransferases; 2. 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 //